2v5l

From Proteopedia

Revision as of 15:38, 30 October 2007

STRUCTURES OF THE OPEN AND CLOSED STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM

Overview

The structure of trypanosomal triosephosphate isomerase (TIM) has been, solved at a resolution of 2.1A in a new crystal form grown at pH 8.8 from, PEG6000. In this new crystal form (space group C2, cell dimensions 94.8 A, 48.3 A, 131.0 A, 90.0 degrees, 100.3 degrees, 90.0 degrees), TIM is, present in a ligand-free state. The asymmetric unit consists of two TIM, subunits. Each of these subunits is part of a dimer which is sitting on a, crystallographic twofold axis, such that the crystal packing is formed, from two TIM dimers in two distinct environments. The two constituent, monomers of a given dimer are, therefore, crystallographically equivalent., In the ligand-free state of TIM in this crystal form, the two types of, dimer are very similar in structure, with the flexible loops in the ... [(full description)]

About this Structure

2V5L is a [Single protein] structure of sequence from [Trypanosoma brucei brucei] with SO4 as [ligand]. Active as [Triose-phosphate isomerase], with EC number [5.3.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism., Noble ME, Zeelen JP, Wierenga RK, Proteins. 1993 Aug;16(4):311-26. PMID:8356028

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