Structural relationship between the mammalian Fe(III)Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatases
The primary structure of uteroferrin (Uf), a 35 kDa monomeric mammalian purple acid phosphatase (PAP) containing a Fe(III)Fe(II) center, has been compared with the sequence of the homodimeric 111 kDa Fe(III)Zn(II) kidney bean purple acid phosphatase (KBPAP). The alignment suggests that the amino a...
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| Veröffentlicht in: | FEBS letters 1995-06, Vol.367 (1), p.56-60 |
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| creator | Klabunde, Thomas Sträter, Norbert Krebs, Bernt Witzel, Herbert |
| description | The primary structure of uteroferrin (Uf), a 35 kDa monomeric mammalian purple acid phosphatase (PAP) containing a Fe(III)Fe(II) center, has been compared with the sequence of the homodimeric 111 kDa Fe(III)Zn(II) kidney bean purple acid phosphatase (KBPAP). The alignment suggests that the amino acid residues ligating the dimetal center are identical in Uf and KBPAP, although the geometry of the coordination sphere might slightly differ. Secondary structure predictions indicate that Uf contains two βαβαβ motifs thus resembling the folding topology of the plant enzyme. Guided by the recently determined X-ray structure of KBPAP a tentative model for the mammalian PAP can be constructed. |
| doi_str_mv | 10.1016/0014-5793(95)00536-I |
| format | Article |
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The alignment suggests that the amino acid residues ligating the dimetal center are identical in Uf and KBPAP, although the geometry of the coordination sphere might slightly differ. Secondary structure predictions indicate that Uf contains two βαβαβ motifs thus resembling the folding topology of the plant enzyme. Guided by the recently determined X-ray structure of KBPAP a tentative model for the mammalian PAP can be constructed.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)00536-I</identifier><identifier>PMID: 7601285</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Acid Phosphatase - chemistry ; Amino Acid Sequence ; Ancestor enzyme ; Animals ; Glycoproteins - chemistry ; Isoenzymes ; KBPAP, kidney bean purple acid phosphatase ; Mammals ; Metalloproteins - chemistry ; Molecular Sequence Data ; Oxygen activation ; PAP, purple acid phosphatase ; Plants - enzymology ; Protein Structure, Secondary ; Purple acid phosphatases ; Sequence Alignment ; Structure prediction ; Tartrate-Resistant Acid Phosphatase ; Uf, uteroferrin</subject><ispartof>FEBS letters, 1995-06, Vol.367 (1), p.56-60</ispartof><rights>1995</rights><rights>FEBS Letters 367 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532I-2a3ba7363f89c51cc3bcc895da9a52bc99769e60f7bc152e53d200d5266ba20b3</citedby><cites>FETCH-LOGICAL-c532I-2a3ba7363f89c51cc3bcc895da9a52bc99769e60f7bc152e53d200d5266ba20b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(95)00536-I$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7601285$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Klabunde, Thomas</creatorcontrib><creatorcontrib>Sträter, Norbert</creatorcontrib><creatorcontrib>Krebs, Bernt</creatorcontrib><creatorcontrib>Witzel, Herbert</creatorcontrib><title>Structural relationship between the mammalian Fe(III)Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatases</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The primary structure of uteroferrin (Uf), a 35 kDa monomeric mammalian purple acid phosphatase (PAP) containing a Fe(III)Fe(II) center, has been compared with the sequence of the homodimeric 111 kDa Fe(III)Zn(II) kidney bean purple acid phosphatase (KBPAP). The alignment suggests that the amino acid residues ligating the dimetal center are identical in Uf and KBPAP, although the geometry of the coordination sphere might slightly differ. Secondary structure predictions indicate that Uf contains two βαβαβ motifs thus resembling the folding topology of the plant enzyme. Guided by the recently determined X-ray structure of KBPAP a tentative model for the mammalian PAP can be constructed.</description><subject>Acid Phosphatase - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Ancestor enzyme</subject><subject>Animals</subject><subject>Glycoproteins - chemistry</subject><subject>Isoenzymes</subject><subject>KBPAP, kidney bean purple acid phosphatase</subject><subject>Mammals</subject><subject>Metalloproteins - chemistry</subject><subject>Molecular Sequence Data</subject><subject>Oxygen activation</subject><subject>PAP, purple acid phosphatase</subject><subject>Plants - enzymology</subject><subject>Protein Structure, Secondary</subject><subject>Purple acid phosphatases</subject><subject>Sequence Alignment</subject><subject>Structure prediction</subject><subject>Tartrate-Resistant Acid Phosphatase</subject><subject>Uf, uteroferrin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1uFDEQhS0ECkPgBiB5hTKLTvwzdrc3SCHKQEuRsgA2bKxqd43GqP-w3YlyEq7CqTgD3T2jZIdYlaveq-fSR8hbzs454_qCMb7JVG7kmVFrxpTUWfmMrHiRy0xudPGcrB4tL8mrGH-wqS-4OSEnuWZcFGpF7r6kMLo0BmhowAaS77u49wOtMN0jdjTtkbbQttB46OgWz8qyXP_59Xt5rSl09WJ5Er53izA00CU6jGFokILzNR32fRz2kCBifE1e7KCJ-OZYT8m37fXXq8_Zze2n8uryJnNKijITICvIpZa7wjjFnZOVc4VRNRhQonLG5NqgZru8clwJVLIWjNVKaF2BYJU8Je8PuUPof44Yk219dNhMx2E_RpvnsthoVUzGzcHoQh9jwJ0dgm8hPFjO7IzbziztzNIaZRfctpzW3h3zx6rF-nHpyHfStwf93jf48F-Zdnv9UczCPDdqmc4ffTgE4UTrzmOw0XnsHNY-oEu27v2_L_0Ls1ajuQ</recordid><startdate>19950619</startdate><enddate>19950619</enddate><creator>Klabunde, Thomas</creator><creator>Sträter, Norbert</creator><creator>Krebs, Bernt</creator><creator>Witzel, Herbert</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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></search><sort><creationdate>19950619</creationdate><title>Structural relationship between the mammalian Fe(III)Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatases</title><author>Klabunde, Thomas ; Sträter, Norbert ; Krebs, Bernt ; Witzel, Herbert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532I-2a3ba7363f89c51cc3bcc895da9a52bc99769e60f7bc152e53d200d5266ba20b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Acid Phosphatase - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Ancestor enzyme</topic><topic>Animals</topic><topic>Glycoproteins - chemistry</topic><topic>Isoenzymes</topic><topic>KBPAP, kidney bean purple acid phosphatase</topic><topic>Mammals</topic><topic>Metalloproteins - chemistry</topic><topic>Molecular Sequence Data</topic><topic>Oxygen activation</topic><topic>PAP, purple acid phosphatase</topic><topic>Plants - enzymology</topic><topic>Protein Structure, Secondary</topic><topic>Purple acid phosphatases</topic><topic>Sequence Alignment</topic><topic>Structure prediction</topic><topic>Tartrate-Resistant Acid Phosphatase</topic><topic>Uf, uteroferrin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Klabunde, Thomas</creatorcontrib><creatorcontrib>Sträter, Norbert</creatorcontrib><creatorcontrib>Krebs, Bernt</creatorcontrib><creatorcontrib>Witzel, Herbert</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Klabunde, Thomas</au><au>Sträter, Norbert</au><au>Krebs, Bernt</au><au>Witzel, Herbert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural relationship between the mammalian Fe(III)Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatases</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-06-19</date><risdate>1995</risdate><volume>367</volume><issue>1</issue><spage>56</spage><epage>60</epage><pages>56-60</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The primary structure of uteroferrin (Uf), a 35 kDa monomeric mammalian purple acid phosphatase (PAP) containing a Fe(III)Fe(II) center, has been compared with the sequence of the homodimeric 111 kDa Fe(III)Zn(II) kidney bean purple acid phosphatase (KBPAP). The alignment suggests that the amino acid residues ligating the dimetal center are identical in Uf and KBPAP, although the geometry of the coordination sphere might slightly differ. Secondary structure predictions indicate that Uf contains two βαβαβ motifs thus resembling the folding topology of the plant enzyme. Guided by the recently determined X-ray structure of KBPAP a tentative model for the mammalian PAP can be constructed.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7601285</pmid><doi>10.1016/0014-5793(95)00536-I</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1995-06, Vol.367 (1), p.56-60 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Acid Phosphatase - chemistry Amino Acid Sequence Ancestor enzyme Animals Glycoproteins - chemistry Isoenzymes KBPAP, kidney bean purple acid phosphatase Mammals Metalloproteins - chemistry Molecular Sequence Data Oxygen activation PAP, purple acid phosphatase Plants - enzymology Protein Structure, Secondary Purple acid phosphatases Sequence Alignment Structure prediction Tartrate-Resistant Acid Phosphatase Uf, uteroferrin |
| title | Structural relationship between the mammalian Fe(III)Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatases |
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