2bes
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(New page: 200px<br /> <applet load="2bes" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bes, resolution 2.10Å" /> '''STRUCTURE OF MYCOBA...)
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Revision as of 18:53, 29 October 2007
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STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, IN COMPLEX WITH 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID.
Overview
Ribose-5-phosphate isomerase (Rpi), an important enzyme in the pentose, phosphate pathway, catalyzes the interconversion of ribulose 5-phosphate, and ribose 5-phosphate. Two unrelated isomerases have been identified, RpiA and RpiB, with different structures and active site residues. The, reaction catalyzed by both enzymes is thought to proceed via a high energy, enediolate intermediate, by analogy to other carbohydrate isomerases. Here, we present studies of RpiB from Mycobacterium tuberculosis together with, small molecules designed to resemble the enediolate intermediate. The, relative affinities of these inhibitors for RpiB have a different pattern, than that observed previously for the RpiA from spinach. X-ray structures, of RpiB in complex with the inhibitors ... [(full description)]
About this Structure
2BES is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with RES as [ligand]. Active as [[1]], with EC number [5.3.1.6]. Full crystallographic information is available from [OCA].
Reference
Competitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanism., Roos AK, Burgos E, Ericsson DJ, Salmon L, Mowbray SL, J Biol Chem. 2005 Feb 25;280(8):6416-22. Epub 2004 Dec 7. PMID:15590681
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