2y6p: Difference between revisions
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[[ | ==EVIDENCE FOR A TWO-METAL-ION-MECHANISM IN THE KDO-CYTIDYLYLTRANSFERASE KDSB== | ||
<StructureSection load='2y6p' size='340' side='right' caption='[[2y6p]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2y6p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y6P OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y6p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y6p RCSB], [http://www.ebi.ac.uk/pdbsum/2y6p PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lipopolysaccharide (LPS) is located on the surface of Gram-negative bacteria and is responsible for maintaining outer membrane stability, which is a prerequisite for cell survival. Furthermore, it represents an important barrier against hostile environmental factors such as antimicrobial peptides and the complement cascade during Gram-negative infections. The sugar 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo) is an integral part of LPS and plays a key role in LPS functionality. Prior to its incorporation into the LPS molecule, Kdo has to be activated by the CMP-Kdo synthetase (CKS). Based on the presence of a single Mg(2+) ion in the active site, detailed models of the reaction mechanism of CKS have been developed previously. Recently, a two-metal-ion hypothesis suggested the involvement of two Mg(2+) ions in Kdo activation. To further investigate the mechanistic aspects of Kdo activation, we kinetically characterized the CKS from the hyperthermophilic organism Aquifex aeolicus. In addition, we determined the crystal structure of this enzyme at a resolution of 2.10 A and provide evidence that two Mg(2+) ions are part of the active site of the enzyme. | |||
Evidence for a Two-Metal-Ion Mechanism in the Cytidyltransferase KdsB, an Enzyme Involved in Lipopolysaccharide Biosynthesis.,Schmidt H, Mesters JR, Wu J, Woodard RW, Hilgenfeld R, Mamat U PLoS One. 2011;6(8):e23231. Epub 2011 Aug 3. PMID:21826242<ref>PMID:21826242</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: 3-deoxy-manno-octulosonate cytidylyltransferase]] | [[Category: 3-deoxy-manno-octulosonate cytidylyltransferase]] | ||
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
Revision as of 10:50, 14 May 2014
EVIDENCE FOR A TWO-METAL-ION-MECHANISM IN THE KDO-CYTIDYLYLTRANSFERASE KDSBEVIDENCE FOR A TWO-METAL-ION-MECHANISM IN THE KDO-CYTIDYLYLTRANSFERASE KDSB
Structural highlights
Publication Abstract from PubMedLipopolysaccharide (LPS) is located on the surface of Gram-negative bacteria and is responsible for maintaining outer membrane stability, which is a prerequisite for cell survival. Furthermore, it represents an important barrier against hostile environmental factors such as antimicrobial peptides and the complement cascade during Gram-negative infections. The sugar 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo) is an integral part of LPS and plays a key role in LPS functionality. Prior to its incorporation into the LPS molecule, Kdo has to be activated by the CMP-Kdo synthetase (CKS). Based on the presence of a single Mg(2+) ion in the active site, detailed models of the reaction mechanism of CKS have been developed previously. Recently, a two-metal-ion hypothesis suggested the involvement of two Mg(2+) ions in Kdo activation. To further investigate the mechanistic aspects of Kdo activation, we kinetically characterized the CKS from the hyperthermophilic organism Aquifex aeolicus. In addition, we determined the crystal structure of this enzyme at a resolution of 2.10 A and provide evidence that two Mg(2+) ions are part of the active site of the enzyme. Evidence for a Two-Metal-Ion Mechanism in the Cytidyltransferase KdsB, an Enzyme Involved in Lipopolysaccharide Biosynthesis.,Schmidt H, Mesters JR, Wu J, Woodard RW, Hilgenfeld R, Mamat U PLoS One. 2011;6(8):e23231. Epub 2011 Aug 3. PMID:21826242[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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