The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins
Bradavidin II is a biotin‐binding protein from Bradyrhizobium japonicum that resembles chicken avidin and bacterial streptavidin. A biophysical characterization was carried out using dynamic light scattering, native mass spectrometry, differential scanning calorimetry, and isothermal titration calor...
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| Veröffentlicht in: | Protein science 2013-07, Vol.22 (7), p.980-994 |
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| creator | Leppiniemi, Jenni Meir, Amit Kähkönen, Niklas Kukkurainen, Sampo Määttä, Juha A. Ojanen, Markus Jänis, Janne Kulomaa, Markku S. Livnah, Oded Hytönen, Vesa P. |
| description | Bradavidin II is a biotin‐binding protein from Bradyrhizobium japonicum that resembles chicken avidin and bacterial streptavidin. A biophysical characterization was carried out using dynamic light scattering, native mass spectrometry, differential scanning calorimetry, and isothermal titration calorimetry combined with structural characterization using X‐ray crystallography. These observations revealed that bradavidin II differs from canonical homotetrameric avidin protein family members in its quaternary structure. In contrast with the other avidins, bradavidin II appears to have a dynamic (transient) oligomeric state in solution. It is monomeric at low protein concentrations but forms higher oligomeric assemblies at higher concentrations. The crystal structure of bradavidin II revealed an important role for Phe42 in shielding the bound ligand from surrounding water molecules, thus functionally replacing the L7,8 loop essential for tight ligand binding in avidin and streptavidin. This bradavidin II characterization opens new avenues for oligomerization‐independent biotin‐binding protein development.
PDB Code(s): Bradavidin II apo Form‐A, 4GGR
Bradavidin II apo Form‐B, 4GGT
Bradavidin II biotin‐complex, 4GGZ |
| doi_str_mv | 10.1002/pro.2281 |
| format | Article |
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PDB Code(s): Bradavidin II apo Form‐A, 4GGR
Bradavidin II apo Form‐B, 4GGT
Bradavidin II biotin‐complex, 4GGZ</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1002/pro.2281</identifier><identifier>PMID: 23661323</identifier><identifier>CODEN: PRCIEI</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Amino Acid Sequence ; Animals ; Biotin - chemistry ; Biotin - metabolism ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Chickens ; Crystal structure ; dynamic structure ; Hydrogen-Ion Concentration ; ligand binding ; Ligands ; Models, Molecular ; Molecular Sequence Data ; oligomeric state ; Protein Binding ; Protein Multimerization ; Protein Unfolding ; Proteins ; Sequence Alignment ; structural cooperativity ; Temperature</subject><ispartof>Protein science, 2013-07, Vol.22 (7), p.980-994</ispartof><rights>Copyright © 2013 The Protein Society</rights><rights>Copyright © 2013 The Protein Society.</rights><rights>Copyright © 2013 The Protein Society 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4381-168d611e6f4f9bf90962ec649a3f6ca43ef44685613074c0a8f09ea367fce58c3</citedby><cites>FETCH-LOGICAL-c4381-168d611e6f4f9bf90962ec649a3f6ca43ef44685613074c0a8f09ea367fce58c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3719091/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3719091/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23661323$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leppiniemi, Jenni</creatorcontrib><creatorcontrib>Meir, Amit</creatorcontrib><creatorcontrib>Kähkönen, Niklas</creatorcontrib><creatorcontrib>Kukkurainen, Sampo</creatorcontrib><creatorcontrib>Määttä, Juha A.</creatorcontrib><creatorcontrib>Ojanen, Markus</creatorcontrib><creatorcontrib>Jänis, Janne</creatorcontrib><creatorcontrib>Kulomaa, Markku S.</creatorcontrib><creatorcontrib>Livnah, Oded</creatorcontrib><creatorcontrib>Hytönen, Vesa P.</creatorcontrib><title>The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>Bradavidin II is a biotin‐binding protein from Bradyrhizobium japonicum that resembles chicken avidin and bacterial streptavidin. A biophysical characterization was carried out using dynamic light scattering, native mass spectrometry, differential scanning calorimetry, and isothermal titration calorimetry combined with structural characterization using X‐ray crystallography. These observations revealed that bradavidin II differs from canonical homotetrameric avidin protein family members in its quaternary structure. In contrast with the other avidins, bradavidin II appears to have a dynamic (transient) oligomeric state in solution. It is monomeric at low protein concentrations but forms higher oligomeric assemblies at higher concentrations. The crystal structure of bradavidin II revealed an important role for Phe42 in shielding the bound ligand from surrounding water molecules, thus functionally replacing the L7,8 loop essential for tight ligand binding in avidin and streptavidin. This bradavidin II characterization opens new avenues for oligomerization‐independent biotin‐binding protein development.
PDB Code(s): Bradavidin II apo Form‐A, 4GGR
Bradavidin II apo Form‐B, 4GGT
Bradavidin II biotin‐complex, 4GGZ</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biotin - chemistry</subject><subject>Biotin - metabolism</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Chickens</subject><subject>Crystal structure</subject><subject>dynamic structure</subject><subject>Hydrogen-Ion Concentration</subject><subject>ligand binding</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>oligomeric state</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Protein Unfolding</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>structural cooperativity</subject><subject>Temperature</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV1LHDEUhkOx1K0t-Ask4E1vxuZrM8mNINKPBcFSLHgXspmT3chMsiYzyv77ZutWbMGrJJyHJ-_hReiYkjNKCPu8yemMMUXfoBkVUjdKy9sDNCNa0kZxqQ7R-1LuCCGCMv4OHTIuJeWMz9DtzRrwOqzW_RZ322iH4HDqwyoNkOu1jHly45QBJ4-X2Xb2IXQh4sUCh4KnGO4nwHZIcYX3kxplhBDLB_TW277Ax_15hH59_XJz-b25uv62uLy4apzgijZUqk5SCtILr5de18gMnBTaci-dFRy8EFLNa1zSCkes8kSD5bL1DubK8SN0_uTdTMsBOgdxzLY3mxwGm7cm2WD-ncSwNqv0YHhL62-0Cj7tBTnVbcpohlAc9L2NkKZiKG-Z1K1WO_T0P_QuTTnW9XYUFXPO5i-ELqdSMvjnMJSYXV31ncyuroqevAz_DP7tpwLNE_AYeti-KjI_fl7_Ef4GSoufew</recordid><startdate>201307</startdate><enddate>201307</enddate><creator>Leppiniemi, Jenni</creator><creator>Meir, Amit</creator><creator>Kähkönen, Niklas</creator><creator>Kukkurainen, Sampo</creator><creator>Määttä, Juha A.</creator><creator>Ojanen, Markus</creator><creator>Jänis, Janne</creator><creator>Kulomaa, Markku S.</creator><creator>Livnah, Oded</creator><creator>Hytönen, Vesa P.</creator><general>Wiley Subscription Services, Inc</general><general>Blackwell Publishing Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7T5</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201307</creationdate><title>The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins</title><author>Leppiniemi, Jenni ; Meir, Amit ; Kähkönen, Niklas ; Kukkurainen, Sampo ; Määttä, Juha A. ; Ojanen, Markus ; Jänis, Janne ; Kulomaa, Markku S. ; Livnah, Oded ; Hytönen, Vesa P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4381-168d611e6f4f9bf90962ec649a3f6ca43ef44685613074c0a8f09ea367fce58c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biotin - chemistry</topic><topic>Biotin - metabolism</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>Chickens</topic><topic>Crystal structure</topic><topic>dynamic structure</topic><topic>Hydrogen-Ion Concentration</topic><topic>ligand binding</topic><topic>Ligands</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>oligomeric state</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Protein Unfolding</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>structural cooperativity</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leppiniemi, Jenni</creatorcontrib><creatorcontrib>Meir, Amit</creatorcontrib><creatorcontrib>Kähkönen, Niklas</creatorcontrib><creatorcontrib>Kukkurainen, Sampo</creatorcontrib><creatorcontrib>Määttä, Juha A.</creatorcontrib><creatorcontrib>Ojanen, Markus</creatorcontrib><creatorcontrib>Jänis, Janne</creatorcontrib><creatorcontrib>Kulomaa, Markku S.</creatorcontrib><creatorcontrib>Livnah, Oded</creatorcontrib><creatorcontrib>Hytönen, Vesa P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leppiniemi, Jenni</au><au>Meir, Amit</au><au>Kähkönen, Niklas</au><au>Kukkurainen, Sampo</au><au>Määttä, Juha A.</au><au>Ojanen, Markus</au><au>Jänis, Janne</au><au>Kulomaa, Markku S.</au><au>Livnah, Oded</au><au>Hytönen, Vesa P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2013-07</date><risdate>2013</risdate><volume>22</volume><issue>7</issue><spage>980</spage><epage>994</epage><pages>980-994</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><coden>PRCIEI</coden><abstract>Bradavidin II is a biotin‐binding protein from Bradyrhizobium japonicum that resembles chicken avidin and bacterial streptavidin. A biophysical characterization was carried out using dynamic light scattering, native mass spectrometry, differential scanning calorimetry, and isothermal titration calorimetry combined with structural characterization using X‐ray crystallography. These observations revealed that bradavidin II differs from canonical homotetrameric avidin protein family members in its quaternary structure. In contrast with the other avidins, bradavidin II appears to have a dynamic (transient) oligomeric state in solution. It is monomeric at low protein concentrations but forms higher oligomeric assemblies at higher concentrations. The crystal structure of bradavidin II revealed an important role for Phe42 in shielding the bound ligand from surrounding water molecules, thus functionally replacing the L7,8 loop essential for tight ligand binding in avidin and streptavidin. This bradavidin II characterization opens new avenues for oligomerization‐independent biotin‐binding protein development.
PDB Code(s): Bradavidin II apo Form‐A, 4GGR
Bradavidin II apo Form‐B, 4GGT
Bradavidin II biotin‐complex, 4GGZ</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>23661323</pmid><doi>10.1002/pro.2281</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Protein science, 2013-07, Vol.22 (7), p.980-994 |
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| subjects | Amino Acid Sequence Animals Biotin - chemistry Biotin - metabolism Carrier Proteins - chemistry Carrier Proteins - metabolism Chickens Crystal structure dynamic structure Hydrogen-Ion Concentration ligand binding Ligands Models, Molecular Molecular Sequence Data oligomeric state Protein Binding Protein Multimerization Protein Unfolding Proteins Sequence Alignment structural cooperativity Temperature |
| title | The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins |
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