5BY2
Sedoheptulose 7-phosphate isomerase from Colwellia psychrerythraea strain 34H
5BY2 の概要
| エントリーDOI | 10.2210/pdb5by2/pdb |
| 分子名称 | Phosphoheptose isomerase (2 entities in total) |
| 機能のキーワード | cpsgmha, sedoheptulose 7-phosphate isomerase, psychrophile, colwellia psychrerythraea strain 34h, isomerase |
| 由来する生物種 | Colwellia psychrerythraea 34H |
| 細胞内の位置 | Cytoplasm : Q47VU0 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 21221.89 |
| 構造登録者 | |
| 主引用文献 | Do, H.,Yun, J.S.,Lee, C.W.,Choi, Y.J.,Kim, H.Y.,Kim, Y.J.,Park, H.,Chang, J.H.,Lee, J.H. Crystal Structure and Comparative Sequence Analysis of GmhA from Colwellia psychrerythraea Strain 34H Provides Insight into Functional Similarity with DiaA Mol.Cells, 38:1086-1095, 2015 Cited by PubMed 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 Å. 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. PubMed: 26612680DOI: 10.14348/molcells.2015.0191 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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