3w1v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:43, 20 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal Structure of Capsular Polysaccharide Synthesizing Enzyme CapE from Staphylococcus aureus in complex with inihibitor==
==Crystal Structure of Capsular Polysaccharide Synthesizing Enzyme CapE from Staphylococcus aureus in complex with inihibitor==
-
<StructureSection load='3w1v' size='340' side='right' caption='[[3w1v]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+
<StructureSection load='3w1v' size='340' side='right'caption='[[3w1v]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3w1v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W1V FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3w1v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1V FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDZ:[(2R,3S,4R,5R,6R)-5-ACETAMIDO-6-[[[(2R,3S,4R,5R)-5-[2,4-BIS(OXIDANYLIDENE)PYRIMIDIN-1-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-3,4-BIS(OXIDANYL)OXAN-2-YL]METHYLIMINO-AZANYLIDENE-AZANIUM'>UDZ</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g5h|4g5h]], [[3vvb|3vvb]], [[3vvc|3vvc]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDZ:[(2R,3S,4R,5R,6R)-5-acetamido-6-[[[(2R,3S,4R,5R)-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,4-bis(oxidanyl)oxan-2-yl]methylimino-azanylidene-azanium'>UDZ</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">capE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 STAAM])</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=3w1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1v OCA], [https://pdbe.org/3w1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1v RCSB], [https://www.ebi.ac.uk/pdbsum/3w1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1v ProSAT]</span></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_4,6-dehydratase_(inverting) UDP-N-acetylglucosamine 4,6-dehydratase (inverting)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.115 4.2.1.115] </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=3w1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1v OCA], [http://pdbe.org/3w1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w1v RCSB], [http://www.ebi.ac.uk/pdbsum/3w1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1v ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/A0A0H3JPH0_STAAM A0A0H3JPH0_STAAM]
-
Enzymes synthesizing the bacterial capsular polysaccharide (CP) are attractive antimicrobial targets. However, we lack critical information about the structure and mechanism of many of them. In an effort to reduce that gap, we have determined three different crystal structures of the enzyme CapE of the human pathogen Staphylococcus aureus. The structure reveals that CapE is a member of the short-chain dehydrogenase/reductase (SDR) super-family of proteins. CapE assembles in a hexameric complex stabilized by three major contact surfaces between protein subunits. Turnover of substrate and/or coenzyme induces major conformational changes at the contact interface between protein subunits, and a displacement of the substrate-binding domain with respect to the Rossmann domain. A novel dynamic element that we called the latch is essential for remodeling of the protein-protein interface. Structural and primary sequence alignment identifies a group of SDR proteins involved in polysaccharide synthesis that share the two salient features of CapE: the mobile loop (latch) and a distinctive catalytic site (MxxxK). The relevance of these structural elements was evaluated by site-directed mutagenesis.
+
-
 
+
-
Crystal structure of the capsular polysaccharide synthesizing protein CapE of Staphylococcus aureus.,Miyafusa T, Caaveiro JM, Tanaka Y, Tanner ME, Tsumoto K Biosci Rep. 2013 Apr 24. PMID:23611437<ref>PMID:23611437</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3w1v" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Staam]]
+
[[Category: Large Structures]]
-
[[Category: Caaveiro, J M]]
+
[[Category: Staphylococcus aureus subsp. aureus Mu50]]
-
[[Category: Miyafusa, T]]
+
[[Category: Caaveiro JM]]
-
[[Category: Tanaka, Y]]
+
[[Category: Miyafusa T]]
-
[[Category: Tsumoto, K]]
+
[[Category: Tanaka Y]]
-
[[Category: Capsular polysaccharide synthesis]]
+
[[Category: Tsumoto K]]
-
[[Category: Epimerase]]
+
-
[[Category: Lyase]]
+
-
[[Category: Oxidase]]
+
-
[[Category: Rossmann fold]]
+
-
[[Category: Short-chain dehydrogenase/reductase]]
+

Current revision

Crystal Structure of Capsular Polysaccharide Synthesizing Enzyme CapE from Staphylococcus aureus in complex with inihibitor

PDB ID 3w1v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools