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2cwq

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(New page: 200px<br /><applet load="2cwq" size="350" color="white" frame="true" align="right" spinBox="true" caption="2cwq, resolution 1.90&Aring;" /> '''Crystal structure of...)
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Revision as of 16:49, 29 January 2008

Image:2cwq.gif

2cwq, resolution 1.90Å

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Crystal structure of conserved protein TTHA0727 from Thermus thermophilus HB8

Overview

TTHA0727 is a conserved hypothetical protein from Thermus thermophilus, HB8, with a molecular mass of 12.6 kDa. TTHA0727 belongs to the, carboxymuconolactone decarboxylase (CMD) family (Pfam 02627). A sequence, comparison with its homologs suggested that TTHA0727 is a distinct protein, from alkylhydroperoxidase AhpD and gamma-carboxymuconolactone, decarboxylase in the CMD family. Here we report the 1.9 A crystal, structure of TTHA0727 (PDB ID: 2CWQ) determined by the multiwavelength, anomalous dispersion method. The TTHA0727 monomer structure consists of, seven alpha-helices (alpha1-alpha7) and one short 3(10)-helix. The crystal, structure and the analytical ultracentrifugation revealed that TTHA0727, forms a hexameric ring structure in solution. The electrostatic potential, distribution on the solvent-accessible surface of the TTHA0727 hexamer, showed that positively charged regions exist on the side of the ring, structure, suggesting that TTHA0727 interacts with some negatively charged, molecules. A structural homology search revealed that the structure of, three alpha-helices (alpha4-alpha6) is remarkably conserved, suggesting, that it is the common structural motif for the CMD family proteins. In, addition, the nine residues of the N-terminal tag bound to the cleft, region between alpha1 and alpha3 in chains A and B of TTHA0727, implying, that this region is the putative binding/active site for some small, molecules.

About this Structure

2CWQ is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the conserved protein TTHA0727 from Thermus thermophilus HB8 at 1.9 A resolution: A CMD family member distinct from carboxymuconolactone decarboxylase (CMD) and AhpD., Ito K, Arai R, Fusatomi E, Kamo-Uchikubo T, Kawaguchi S, Akasaka R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S, Protein Sci. 2006 May;15(5):1187-92. Epub 2006 Apr 5. PMID:16597838

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