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Crystal structure and comparative sequence analysis of GmhA from Colwellia psychrerythraea strain 34H provides insight into functional similarity with DiaA

Cited 5 time in scopus
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Title
Crystal structure and comparative sequence analysis of GmhA from Colwellia psychrerythraea strain 34H provides insight into functional similarity with DiaA
Other Titles
호냉성 박테리아 (Colwellia psychrerythraea) 유래 GmhA 단백질의 구조 및 서열 분석을 통한 DiaA 단백질과의 비교연구
Authors
Hackwon Do
Lee, Jun Hyuck
Jeong Ho Chang
Park, Hyun
Youn-Jung Kim
Hye-Yeon Kim
Young Jun Choi
Lee, Chang Woo
Ji-Sook Yun
Subject
Biochemistry & Molecular Biology; Cell Biology
Keywords
Colwellia psychrerythraea strain 34H; CpsGmhA; Psychrophile; Sedoheptulose 7-phosphate isomerase; X-ray crystallography
Issue Date
2015
Citation
Hackwon Do, et al. 2015. "Crystal structure and comparative sequence analysis of GmhA from Colwellia psychrerythraea strain 34H provides insight into functional similarity with DiaA". MOLECULES AND CELLS, 38(12): 1086-1095.
Abstract
The psychrophilic organism Colwellia psychrerythraea strain 34H produces extracellular polysaccharide substances to tolerate cold environments. Sedoheptulose 7-phosphate isomerase (GmhA) is essential for producing D-glycero-D-mannoheptose 7-phosphate, a key mediator in the lipopolysaccharide biosynthetic pathway. We determined the crystal structure of GmhA from C. psychrerythraea strain 34H (CpsGmhA, UniProtKB code: Q47VU0) at a resolution of 2.8 A. The tetrameric structure is similar to that of homologous GmhA structures. Interestingly, one of the catalytic residues, glutamate, which has been reported to be critical for the activity of other homologous GmhA enzymes, is replaced by a glutamine residue in the CpsGmhA protein. We also found differences in the conformations of several other catalytic residues. Extensive structural and sequence analyses reveal that CpsGmhA shows high similarity to Escherichia coli DnaA initiator-associating protein A (DiaA). Therefore, the CpsGmhA structure reported here may provide insight into the structural and functional correlations between GmhA and DiaA among specific microorganisms.
URI
http://repository.kopri.re.kr/handle/201206/6475
DOI
http://dx.doi.org/10.14348/molcells.2015.0191
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