1wvo

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.

Structural highlights

1wvo is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

SIAS_HUMAN Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of the C-terminal antifreeze-like (AFL) domain of human sialic acid synthase was determined by NMR spectroscopy. The structure comprises one alpha- and two single-turn 3(10)-helices and two beta-strands, and is similar to those of the type III antifreeze proteins. Evolutionary trace analyses of the type III antifreeze protein family suggested that the class-specific residues in the human and bacterial AFL domains are important for their substrate binding, while the class-specific residues of the fish antifreeze proteins are gathered on the ice-binding surface.

Solution structure of the antifreeze-like domain of human sialic acid synthase.,Hamada T, Ito Y, Abe T, Hayashi F, Guntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, Hirota H Protein Sci. 2006 May;15(5):1010-6. Epub 2006 Apr 5. PMID:16597820^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hamada T, Ito Y, Abe T, Hayashi F, Guntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, Hirota H. Solution structure of the antifreeze-like domain of human sialic acid synthase. Protein Sci. 2006 May;15(5):1010-6. Epub 2006 Apr 5. PMID:16597820 doi:10.1110/ps.051700406

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wvo"

@@ Line 1: / Line 1: @@
 ==Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.==
-<StructureSection load='1wvo' size='340' side='right'caption='[[1wvo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1wvo' size='340' side='right'caption='[[1wvo]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wvo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wvo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVO FirstGlance]. <br>
-</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=1wvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wvo OCA], [https://pdbe.org/1wvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wvo RCSB], [https://www.ebi.ac.uk/pdbsum/1wvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wvo ProSAT], [https://www.topsan.org/Proteins/RSGI/1wvo TOPSAN]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1wvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wvo OCA], [https://pdbe.org/1wvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wvo RCSB], [https://www.ebi.ac.uk/pdbsum/1wvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wvo ProSAT], [https://www.topsan.org/Proteins/RSGI/1wvo TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SIAS_HUMAN SIAS_HUMAN]] Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.
+[https://www.uniprot.org/uniprot/SIAS_HUMAN SIAS_HUMAN] Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Hamada, T]]
+[[Category: Hamada T]]
-[[Category: Hayashi, F]]
+[[Category: Hayashi F]]
-[[Category: Hirota, H]]
+[[Category: Hirota H]]
-[[Category: Ito, Y]]
+[[Category: Ito Y]]
-[[Category: Structural genomic]]
+[[Category: Yokoyama S]]
-[[Category: Yokoyama, S]]
-[[Category: Antifreeze protein like domain]]
-[[Category: N-acetylneuraminic acid phosphate synthase]]
-[[Category: National project on protein structural and functional analyse]]
-[[Category: Nppsfa]]
-[[Category: Rsgi]]
-[[Category: Transferase]]

1wvo

From Proteopedia

Current revision

Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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