1weh

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Revision as of 21:42, 24 November 2007

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spinqualitylabelsall models 1weh, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the conserved hypothetical protein TT1887 from Thermus thermophilus HB8

Overview

TT1887 and TT1465 from Thermus thermophilus HB8 are conserved hypothetical, proteins, and are annotated as possible lysine decarboxylases in the Pfam, database. Here we report the crystal structures of TT1887 and TT1465 at, 1.8 A and 2.2 A resolutions, respectively, as determined by the, multiwavelength anomalous dispersion (MAD) method. TT1887 is a, homotetramer, while TT1465 is a homohexamer in the crystal and in, solution. The structures of the TT1887 and TT1465 monomers contain single, domains with the Rossmann fold, comprising six alpha helices and seven, beta strands, and are quite similar to each other. The major structural, differences exist in the N terminus of TT1465, where there are two, additional alpha helices. A comparison of the structures revealed the, elements that are responsible for the different oligomerization modes. The, distributions of the electrostatic potential on the solvent-accessible, surfaces suggested putative active sites.

About this Structure

1WEH is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8., Kukimoto-Niino M, Murayama K, Kato-Murayama M, Idaka M, Bessho Y, Tatsuguchi A, Ushikoshi-Nakayama R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S, Protein Sci. 2004 Nov;13(11):3038-42. Epub 2004 Sep 30. PMID:15459330

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