1usl

From Proteopedia

Revision as of 14:05, 30 October 2007

STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, COMPLEXED WITH PHOSPHATE.

Overview

Ribose-5-phosphate isomerases (EC 5.3.1.6) inter-convert, ribose-5-phosphate and ribulose-5-phosphate. This reaction allows the, synthesis of ribose from other sugars, as well a means for salvage of, carbohydrates after nucleotide breakdown. Two unrelated types of enzyme, are known to catalyze the isomerization. The most common one, RpiA, is, present in almost all organisms. The second type, RpiB, is found in many, bacterial species.Here, we demonstrate that the RpiB from Mycobacterium, tuberculosis (Rv2465c) has catalytic properties very similar to those, previously reported for the Escherichia coli RpiB enzyme. Further, we, report the structure of the mycobacterial enzyme, solved by molecular, replacement and refined to 1.88A resolution. Comparison with the E.coli, structure shows that ... [(full description)]

About this Structure

1USL is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with PO4 as [ligand]. Active as [Ribose-5-phosphate isomerase], with EC number [5.3.1.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site., Roos AK, Andersson CE, Bergfors T, Jacobsson M, Karlen A, Unge T, Jones TA, Mowbray SL, J Mol Biol. 2004 Jan 16;335(3):799-809. PMID:14687575

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