This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1h7h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

Revision as of 13:55, 18 December 2007

Image:1h7h.gif

1h7h, resolution 2.3Å

Drag the structure with the mouse to rotate

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

Overview

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 Structure

1H7H is a Single protein structure of sequence from Escherichia coli with CDP as ligand. Active as 3-deoxy-manno-octulosonate cytidylyltransferase, with EC number 2.7.7.38 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

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 Tue Dec 18 16:05:24 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h7h"
Personal tools