1h7f: Difference between revisions

Revision as of 18:31, 2 May 2008

THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE AND OF ITS COMPLEXES WITH SUBSTRATES AND SUBSTRATE ANALOGUES, CMP COMPLEX

OverviewOverview

The enzyme CMP-Kdo synthetase (CKS) catalyzes the activation of the sugar Kdo (2-keto-3-deoxy-manno-octonic acid) by forming a monophosphate diester. CKS is a pharmaceutical target because CMP-Kdo is used in the biosynthesis of lipopolysaccharides that are vital for Gram-negative bacteria. We have refined the structure of the unligated capsule-specific CKS from Escherichia coli at 1.8 A resolution (1 A=0.1 nm) and we have established the structures of its complexes with the substrate CTP, with CDP and CMP as well as with the product analog CMP-NeuAc (CMP-sialate) by X-ray diffraction analyses at resolutions between 2.1 A and 2.5 A. The N-terminal domains of the dimeric enzyme bind CTP in a peculiar nucleotide-binding fold, whereas the C-terminal domains form the dimer interface. The observed binding geometries together with the amino acid variabilities during evolution and the locations of a putative Mg(2+) and of a very strongly bound water molecule suggest a pathway for the catalysis. The N-terminal domain shows sequence homology with the CMP-NeuAc synthetases. Moreover, the chain fold and the substrate-binding position of CKS resemble those of other enzymes processing nucleotide-sugars.

About this StructureAbout this Structure

1H7F is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The structure of CMP:2-keto-3-deoxy-manno-octonic acid synthetase and of its complexes with substrates and substrate analogs., Jelakovic S, Schulz GE, J Mol Biol. 2001 Sep 7;312(1):143-55. PMID:11545592 Page seeded by OCA on Fri May 2 18:31:58 2008

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OCA

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 [[Image:1h7f.gif|left|200px]]
- {{Structure
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+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38] </span>
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-|GENE= KPSU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+-->
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-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7f OCA], [http://www.ebi.ac.uk/pdbsum/1h7f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h7f RCSB]</span>
-}}
 '''THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE AND OF ITS COMPLEXES WITH SUBSTRATES AND SUBSTRATE ANALOGUES, CMP COMPLEX'''
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 [[Category: Jelakovic, S.]]
 [[Category: Schulz, G E.]]
-[[Category: cmp-kdo synthetase]]
+[[Category: Cmp-kdo synthetase]]
-[[Category: lipopolysaccharide biosynthesis]]
+[[Category: Lipopolysaccharide biosynthesis]]
-[[Category: nucleoside monophosphate glycoside]]
+[[Category: Nucleoside monophosphate glycoside]]
-[[Category: sugar-activating enzyme]]
+[[Category: Sugar-activating enzyme]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:31:58 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:20 2008''