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Crystal structure of LeuD from Methanococcus jannaschii

Authors
Lee, Eun HyeCho, Yong WookHwang, Kwang Yeon
Issue Date
9-Mar-2012
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
LeuD; 3-Isopropylmalate isomerase; 3-lsopropylmalate dehydratase; Small subunit; Broad specificity; Crystal structure
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.419, no.2, pp.160 - 164
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
419
Number
2
Start Page
160
End Page
164
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/105307
DOI
10.1016/j.bbrc.2012.01.125
ISSN
0006-291X
Abstract
3-Isopropylmalate/citramalate (IPM) isomerase catalyzes the second step in the leucine biosynthesis pathway. IPM isomerase from Methanococcus jannaschii is a complex protein consisting of a large (MjLeuC) and a small subunit (MjLeuD). It has broad substrate specificity, unlike other bacterial IPM isomerases. In order to understand the reasons for this broad substrate specificity, we determined the crystal structure of MjLeuD at a resolution of 2.0 angstrom. The asymmetric unit contained 6 molecules of LeuD, including three homodimers. The overall structure had a beta/beta/alpha sandwich-fold consisting of 8 alpha-helices and 7 beta-strands. The C-terminal helix, which is important in homodimer formation, showed conformational differences between two homodimer forms of MjLeuD. In addition, we identified a hydrophobic residue (Val28) near the substrate recognition region that may explain the broad substrate specificity of IPM isomerase. Therefore, we suggest that LeuD proteins can be divided into 2 subfamilies, LeuD subfamilies 1 and 2, which show differences in overall structure and in the substrate recognition region. (C) 2012 Elsevier Inc. All rights reserved.
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