2z87
From Proteopedia
(Difference between revisions)
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<StructureSection load='2z87' size='340' side='right'caption='[[2z87]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='2z87' size='340' side='right'caption='[[2z87]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2z87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2z87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z87 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UD2:URIDINE-DIPHOSPHATE-N-ACETYLGALACTOSAMINE'>UD2</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=2z87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z87 OCA], [https://pdbe.org/2z87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z87 RCSB], [https://www.ebi.ac.uk/pdbsum/2z87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z87 ProSAT]</span></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=2z87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z87 OCA], [https://pdbe.org/2z87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z87 RCSB], [https://www.ebi.ac.uk/pdbsum/2z87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z87 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CHS_ECOLX CHS_ECOLX] Glycosyltransferase that catalyzes elongation of chondroitin, a polysaccharide composed of a repeating disaccharide of N-acetylgalactosamine (GalNAc) and glucuronic acid (GlcUA) units, by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. Each chondroitin unit has the composition beta-(1->4)-GlcUA-beta-(1->3)-GalNAc.<ref>PMID:11943778</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z87 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z87 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Elongation of glycosaminoglycan chains, such as heparan and chondroitin, is catalyzed by bi-functional glycosyltransferases, for which both 3-dimensional structures and reaction mechanisms remain unknown. The bacterial chondroitin polymerase K4CP catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. Here, we have determined the crystal structure of K4CP in the presence of UDP and UDP-GalNAc as well as with UDP and UDP-GlcUA. The structures consisted of two GT-A fold domains in which the two active sites were 60A apart. UDP-GalNAc and UDP-GlcUA were found at the active sites of the N-terminal and C-terminal domains, respectively. The present K4CP structures have provided the structural basis for further investigating the molecular mechanism of biosynthesis of chondroitin chain. | ||
- | |||
- | Crystal structure of chondroitin polymerase from Escherichia coli K4.,Osawa T, Sugiura N, Shimada H, Hirooka R, Tsuji A, Shirakawa T, Fukuyama K, Kimura M, Kimata K, Kakuta Y Biochem Biophys Res Commun. 2009 Jan 2;378(1):10-4. Epub 2008 Sep 2. PMID:18771653<ref>PMID:18771653</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2z87" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Hirooka | + | [[Category: Hirooka R]] |
- | [[Category: Kakuta | + | [[Category: Kakuta Y]] |
- | [[Category: Kimata | + | [[Category: Kimata K]] |
- | [[Category: Kimura | + | [[Category: Kimura M]] |
- | [[Category: Osawa | + | [[Category: Osawa T]] |
- | [[Category: Shimada | + | [[Category: Shimada H]] |
- | [[Category: Sugiura | + | [[Category: Sugiura N]] |
- | [[Category: Tsuji | + | [[Category: Tsuji A]] |
- | + |
Current revision
Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP
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Categories: Escherichia coli | Large Structures | Hirooka R | Kakuta Y | Kimata K | Kimura M | Osawa T | Shimada H | Sugiura N | Tsuji A