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1gkz

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[[Category: potassium]]
[[Category: potassium]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:24:43 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:14:36 2007''

Revision as of 13:09, 30 October 2007


1gkz, resolution 2.20Å

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BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE KINASE (BCK) COMPLXED WITH ADP

Overview

Mitochondrial protein kinases (mPKs) are molecular switches that, down-regulate the oxidation of branched-chain alpha-ketoacids and, pyruvate. Elevated levels of these metabolites are implicated in disease, states such as insulin-resistant Type II diabetes, branched-chain, ketoaciduria, and primary lactic acidosis. We report a three-dimensional, structure of a member of the mPK family, rat branched-chain alpha-ketoacid, dehydrogenase kinase (BCK). BCK features a characteristic, nucleotide-binding domain and a four-helix bundle domain. These two, domains are reminiscent of modules found in protein histidine kinases, (PHKs), which are involved in two-component signal transduction systems., Unlike PHKs, BCK dimerizes through direct interaction of two opposing, nucleotide-binding domains. ... [(full description)]

About this Structure

1GKZ is a [Single protein] structure of sequence from [Rattus norvegicus] with MG, K, CL, XE and ADP as [ligands]. Active as [Transferred entry: 2.7.11.4], with EC number [2.7.1.115]. Structure known Active Site: K. Full crystallographic information is available from [OCA].

Reference

Structure of rat BCKD kinase: nucleotide-induced domain communication in a mitochondrial protein kinase., Machius M, Chuang JL, Wynn RM, Tomchick DR, Chuang DT, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11218-23. Epub 2001 Sep 18. PMID:11562470

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