Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family
Sucrose non-fermenting (Snf1)-related kinase (SNRK) is a novel member of the AMP-activated protein kinase (AMPK) family and is involved in many metabolic processes. Here we report the crystal structure of an N-terminal SNRK fragment containing kinase and adjacent ubiquitin-associated (UBA) domains....
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| Veröffentlicht in: | Biochemical and biophysical research communications 2018-01, Vol.495 (1), p.1-6 |
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| creator | Wang, Yu-Lu Wang, Jue Chen, Xiang Wang, Zhi-Xin Wu, Jia-Wei |
| description | Sucrose non-fermenting (Snf1)-related kinase (SNRK) is a novel member of the AMP-activated protein kinase (AMPK) family and is involved in many metabolic processes. Here we report the crystal structure of an N-terminal SNRK fragment containing kinase and adjacent ubiquitin-associated (UBA) domains. This structure shows that the UBA domain binds between the N- and C-lobes of the kinase domain. The mode of UBA binding in SNRK largely resembles that in AMPK and brain specific kinase (BRSK), however, unique interactions play vital roles in stabilizing the KD-UBA interface of SNRK. We further propose a potential role of the UBA domain in the regulation of SNRK kinase activity. This study provides new insights into the structural diversities of the AMPK kinase family.
•The UBA domain of SNRK binds between the N- and C-lobes of the kinase domain.•The UBA binding mode in SNRK is similar to yet different from AMPK.•Structural analyses suggested an inhibitory function of SNRK UBA domain. |
| doi_str_mv | 10.1016/j.bbrc.2017.10.105 |
| format | Article |
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•The UBA domain of SNRK binds between the N- and C-lobes of the kinase domain.•The UBA binding mode in SNRK is similar to yet different from AMPK.•Structural analyses suggested an inhibitory function of SNRK UBA domain.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2017.10.105</identifier><identifier>PMID: 29061304</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; Amino Acid Sequence ; AMP ; AMP-Activated Protein Kinases - chemistry ; AMP-Activated Protein Kinases - metabolism ; AMPK family ; Animals ; BRAIN ; Catalytic Domain ; CRYSTAL STRUCTURE ; Crystallography, X-Ray ; Humans ; KD-UBA ; Models, Molecular ; Protein Domains ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Receptor, EphA5 - chemistry ; Receptor, EphA5 - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; SACCHAROSE ; Sequence Homology, Amino Acid ; SNRK ; Structural diversity ; Ubiquitin - metabolism</subject><ispartof>Biochemical and biophysical research communications, 2018-01, Vol.495 (1), p.1-6</ispartof><rights>2017 Elsevier Inc.</rights><rights>Copyright © 2017 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c384t-9904ec81f197c9d3cdabd82a52dd7579e0f94ff2e648984978ab7d10c498dddc3</citedby><cites>FETCH-LOGICAL-c384t-9904ec81f197c9d3cdabd82a52dd7579e0f94ff2e648984978ab7d10c498dddc3</cites><orcidid>0000-0002-0168-2352</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2017.10.105$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29061304$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/23134082$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Yu-Lu</creatorcontrib><creatorcontrib>Wang, Jue</creatorcontrib><creatorcontrib>Chen, Xiang</creatorcontrib><creatorcontrib>Wang, Zhi-Xin</creatorcontrib><creatorcontrib>Wu, Jia-Wei</creatorcontrib><title>Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Sucrose non-fermenting (Snf1)-related kinase (SNRK) is a novel member of the AMP-activated protein kinase (AMPK) family and is involved in many metabolic processes. Here we report the crystal structure of an N-terminal SNRK fragment containing kinase and adjacent ubiquitin-associated (UBA) domains. This structure shows that the UBA domain binds between the N- and C-lobes of the kinase domain. The mode of UBA binding in SNRK largely resembles that in AMPK and brain specific kinase (BRSK), however, unique interactions play vital roles in stabilizing the KD-UBA interface of SNRK. We further propose a potential role of the UBA domain in the regulation of SNRK kinase activity. This study provides new insights into the structural diversities of the AMPK kinase family.
•The UBA domain of SNRK binds between the N- and C-lobes of the kinase domain.•The UBA binding mode in SNRK is similar to yet different from AMPK.•Structural analyses suggested an inhibitory function of SNRK UBA domain.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Amino Acid Sequence</subject><subject>AMP</subject><subject>AMP-Activated Protein Kinases - chemistry</subject><subject>AMP-Activated Protein Kinases - metabolism</subject><subject>AMPK family</subject><subject>Animals</subject><subject>BRAIN</subject><subject>Catalytic Domain</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography, X-Ray</subject><subject>Humans</subject><subject>KD-UBA</subject><subject>Models, Molecular</subject><subject>Protein Domains</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Receptor, EphA5 - chemistry</subject><subject>Receptor, EphA5 - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>SACCHAROSE</subject><subject>Sequence Homology, Amino Acid</subject><subject>SNRK</subject><subject>Structural diversity</subject><subject>Ubiquitin - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUuP1DAQhC0EYoeFP8ABWeLCJUPbcR6WuAwjXtrlIWAlbpZjd1gPib3Yzkrz70kmC0dOLXV_VSp1EfKUwZYBq18etl0XzZYDa7anXXWPbBhIKDgDcZ9sAKAuuGQ_zsijlA4AjIlaPiRnXELNShAb4vfxmLIeaMpxMnmKSENP8zXSX87rhFR7S69e76gNo3Y-Lddvn75e0Ii3qIdENbUuZedNPmGd89b5n3QMFqnzJ6fdxy8XtNejG46PyYN-VuGTu3lOrt6--b5_X1x-fvdhv7ssTNmKXEgJAk3LeiYbI21prO5sy3XFrW2qRiL0UvQ9x1q0shWyaXXXWAZGyNZaa8pz8nz1DXM2lYzLaK5N8B5NVrxkpYCWz9SLlbqJ4feEKavRJYPDoD2GKSkmqwrquuViRvmKmhhSitirm-hGHY-KgVraUAe1tKGWNtZdNYue3flP3Yj2n-Tv-2fg1Qrg_Itbh3GJit6gdXFJaoP7n_8feB-ZoA</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Wang, Yu-Lu</creator><creator>Wang, Jue</creator><creator>Chen, Xiang</creator><creator>Wang, Zhi-Xin</creator><creator>Wu, Jia-Wei</creator><general>Elsevier Inc</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>7X8</scope><scope>OTOTI</scope><orcidid>https://orcid.org/0000-0002-0168-2352</orcidid></search><sort><creationdate>20180101</creationdate><title>Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family</title><author>Wang, Yu-Lu ; Wang, Jue ; Chen, Xiang ; Wang, Zhi-Xin ; Wu, Jia-Wei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c384t-9904ec81f197c9d3cdabd82a52dd7579e0f94ff2e648984978ab7d10c498dddc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Amino Acid Sequence</topic><topic>AMP</topic><topic>AMP-Activated Protein Kinases - chemistry</topic><topic>AMP-Activated Protein Kinases - metabolism</topic><topic>AMPK family</topic><topic>Animals</topic><topic>BRAIN</topic><topic>Catalytic Domain</topic><topic>CRYSTAL STRUCTURE</topic><topic>Crystallography, X-Ray</topic><topic>Humans</topic><topic>KD-UBA</topic><topic>Models, Molecular</topic><topic>Protein Domains</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Receptor, EphA5 - chemistry</topic><topic>Receptor, EphA5 - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>SACCHAROSE</topic><topic>Sequence Homology, Amino Acid</topic><topic>SNRK</topic><topic>Structural diversity</topic><topic>Ubiquitin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Yu-Lu</creatorcontrib><creatorcontrib>Wang, Jue</creatorcontrib><creatorcontrib>Chen, Xiang</creatorcontrib><creatorcontrib>Wang, Zhi-Xin</creatorcontrib><creatorcontrib>Wu, Jia-Wei</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Yu-Lu</au><au>Wang, Jue</au><au>Chen, Xiang</au><au>Wang, Zhi-Xin</au><au>Wu, Jia-Wei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2018-01-01</date><risdate>2018</risdate><volume>495</volume><issue>1</issue><spage>1</spage><epage>6</epage><pages>1-6</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Sucrose non-fermenting (Snf1)-related kinase (SNRK) is a novel member of the AMP-activated protein kinase (AMPK) family and is involved in many metabolic processes. Here we report the crystal structure of an N-terminal SNRK fragment containing kinase and adjacent ubiquitin-associated (UBA) domains. This structure shows that the UBA domain binds between the N- and C-lobes of the kinase domain. The mode of UBA binding in SNRK largely resembles that in AMPK and brain specific kinase (BRSK), however, unique interactions play vital roles in stabilizing the KD-UBA interface of SNRK. We further propose a potential role of the UBA domain in the regulation of SNRK kinase activity. This study provides new insights into the structural diversities of the AMPK kinase family.
•The UBA domain of SNRK binds between the N- and C-lobes of the kinase domain.•The UBA binding mode in SNRK is similar to yet different from AMPK.•Structural analyses suggested an inhibitory function of SNRK UBA domain.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>29061304</pmid><doi>10.1016/j.bbrc.2017.10.105</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0002-0168-2352</orcidid></addata></record> |
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| subjects | 60 APPLIED LIFE SCIENCES Amino Acid Sequence AMP AMP-Activated Protein Kinases - chemistry AMP-Activated Protein Kinases - metabolism AMPK family Animals BRAIN Catalytic Domain CRYSTAL STRUCTURE Crystallography, X-Ray Humans KD-UBA Models, Molecular Protein Domains Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Receptor, EphA5 - chemistry Receptor, EphA5 - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism SACCHAROSE Sequence Homology, Amino Acid SNRK Structural diversity Ubiquitin - metabolism |
| title | Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family |
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