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| | <StructureSection load='4cyf' size='340' side='right'caption='[[4cyf]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='4cyf' size='340' side='right'caption='[[4cyf]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cyf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CYF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cyf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CYF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyf OCA], [https://pdbe.org/4cyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cyf RCSB], [https://www.ebi.ac.uk/pdbsum/4cyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cyf ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cyg|4cyg]], [[4cyu|4cyu]]</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantetheine_hydrolase Pantetheine hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.92 3.5.1.92] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyf OCA], [http://pdbe.org/4cyf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cyf RCSB], [http://www.ebi.ac.uk/pdbsum/4cyf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cyf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VNN1_HUMAN VNN1_HUMAN]] Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine.<ref>PMID:10567687</ref> <ref>PMID:11491533</ref> | + | [[https://www.uniprot.org/uniprot/VNN1_HUMAN VNN1_HUMAN]] Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine.<ref>PMID:10567687</ref> <ref>PMID:11491533</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pantetheine hydrolase]]
| + | [[Category: Adams TE]] |
| - | [[Category: Adams, T E]] | + | [[Category: Boersma YL]] |
| - | [[Category: Boersma, Y L]] | + | [[Category: Bozaoglu K]] |
| - | [[Category: Bozaoglu, K]] | + | [[Category: Cowieson N]] |
| - | [[Category: Cowieson, N]] | + | [[Category: Krippner G]] |
| - | [[Category: Krippner, G]] | + | [[Category: Lucent D]] |
| - | [[Category: Lucent, D]] | + | [[Category: Newman J]] |
| - | [[Category: Newman, J]] | + | [[Category: Peat TS]] |
| - | [[Category: Peat, T S]] | + | [[Category: Sparrow L]] |
| - | [[Category: Sparrow, L]] | + | |
| - | [[Category: Coa biosynthesis oxidative stress]]
| + | |
| - | [[Category: Colitis]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inflammation]]
| + | |
| Structural highlights
Function
[VNN1_HUMAN] Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine.[1] [2]
Publication Abstract from PubMed
Although part of the coenzyme A pathway, vanin 1 (also known as pantetheinase) sits on the cell surface of many cell types as an ectoenzyme, catalyzing the breakdown of pantetheine to pantothenic acid (vitamin B5) and cysteamine, a strong reducing agent. Vanin 1 was initially discovered as a protein involved in the homing of leukocytes to the thymus. Numerous studies have shown that vanin 1 is involved in inflammation, and more recent studies have shown a key role in metabolic disease. Here, the X-ray crystal structure of human vanin 1 at 2.25 A resolution is presented, which is the first reported structure from the vanin family, as well as a crystal structure of vanin 1 bound to a specific inhibitor. These structures illuminate how vanin 1 can mediate its biological roles by way of both enzymatic activity and protein-protein interactions. Furthermore, it sheds light on how the enzymatic activity is regulated by a novel allosteric mechanism at a domain interface.
The structure of vanin 1: a key enzyme linking metabolic disease and inflammation.,Boersma YL, Newman J, Adams TE, Cowieson N, Krippner G, Bozaoglu K, Peat TS Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3320-9. doi:, 10.1107/S1399004714022767. Epub 2014 Nov 28. PMID:25478849[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Maras B, Barra D, Dupre S, Pitari G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 1999 Nov 19;461(3):149-52. PMID:10567687
- ↑ Martin F, Malergue F, Pitari G, Philippe JM, Philips S, Chabret C, Granjeaud S, Mattei MG, Mungall AJ, Naquet P, Galland F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics. 2001 May-Jun;53(4):296-306. PMID:11491533
- ↑ Boersma YL, Newman J, Adams TE, Cowieson N, Krippner G, Bozaoglu K, Peat TS. The structure of vanin 1: a key enzyme linking metabolic disease and inflammation. Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3320-9. doi:, 10.1107/S1399004714022767. Epub 2014 Nov 28. PMID:25478849 doi:http://dx.doi.org/10.1107/S1399004714022767
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