1nog

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(New page: 200px<br /><applet load="1nog" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nog, resolution 1.55&Aring;" /> '''Crystal Structure of...)
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Revision as of 21:21, 24 November 2007

Image:1nog.gif

1nog, resolution 1.55Å

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Crystal Structure of Conserved Protein 0546 from Thermoplasma Acidophilum

Overview

ATP:cobalamin adenosyltransferase MMAB was recently identified as the gene, responsible for a disorder of cobalamin metabolism in humans (cblB, complementation group). The crystal structure of the MMAB sequence, homologue from Thermoplasma acidophilum (TA1434; GenBank identification, number gi|16082403) was determined to a resolution of 1.5 A. TA1434 was, confirmed to be an ATP:cobalamin adenosyltransferase, which depended, absolutely on divalent metal ions (Mg2+ > Mn2+ > Co2+) and only used ATP, or dATP as adenosyl donors. The apparent Km of TA1434 was 110 microM (kcat, = 0.23 s(-1)) for ATP, 140 microM (kcat = 0.11 s(-1)) for dATP, and 3, microM (kcat = 0.18 s(-1)) for cobalamin. TA1434 is a trimer in solution, and in the crystal structure, with each subunit composed of a five-helix, bundle. The location of disease-related point mutations and other residues, conserved among the homologues of TA1434 suggest that the active site lies, at the junctions between the subunits. Mutations in TA1434 that correspond, to the disease-related mutations resulted in proteins that were inactive, for ATP:cobalamin adenosyltransferase activity in vitro, confirming that, these mutations define the molecular basis of the human disease.

About this Structure

1NOG is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.

Reference

The structural basis for methylmalonic aciduria. The crystal structure of archaeal ATP:cobalamin adenosyltransferase., Saridakis V, Yakunin A, Xu X, Anandakumar P, Pennycooke M, Gu J, Cheung F, Lew JM, Sanishvili R, Joachimiak A, Arrowsmith CH, Christendat D, Edwards AM, J Biol Chem. 2004 May 28;279(22):23646-53. Epub 2004 Mar 25. PMID:15044458

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