Crystal Structure and Comparative Sequence Analysis of GmhA from Colwellia psychrerythraea Strain 34H Provides Insight into Functional Similarity with DiaA
| Autor: | Ji-Sook Yun, Jeong Ho Chang, Hye Yeon Kim, Hackwon Do, Chang Woo Lee, Hyun June Park, Young Jun Choi, Youn-Jung Kim, Jun Hyuck Lee |
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| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular psychrophile Protein Conformation Sequence analysis Glutamine Racemases and Epimerases Isomerase Biology Crystallography X-Ray medicine.disease_cause Article chemistry.chemical_compound Protein structure Bacterial Proteins Sequence Analysis Protein CpsGmhA Catalytic Domain medicine Cloning Molecular DiaA Molecular Biology Escherichia coli sedoheptulose 7-phosphate isomerase chemistry.chemical_classification Strain (chemistry) Cell Biology General Medicine DnaA Sedoheptulose Enzyme chemistry Biochemistry Structural Homology Protein Colwellia psychrerythraea strain 34H Carrier Proteins Gammaproteobacteria |
| Zdroj: | Molecules and Cells |
| ISSN: | 0219-1032 1016-8478 |
| DOI: | 10.14348/molcells.2015.0191 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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