5BY2

Sedoheptulose 7-phosphate isomerase from Colwellia psychrerythraea strain 34H

Summary for 5BY2

• Entry DOI: 10.2210/pdb5by2/pdb
• Descriptor: Phosphoheptose isomerase (2 entities in total)
• Functional Keywords: cpsgmha, sedoheptulose 7-phosphate isomerase, psychrophile, colwellia psychrerythraea strain 34h, isomerase
• Biological source: Colwellia psychrerythraea 34H
• Cellular location: Cytoplasm : Q47VU0
• Total number of polymer chains: 1
• Total formula weight: 21221.89

Authors

Lee, J.H.,Chang, J.H.,Do, H.,Yun, J.S. (deposition date: 2015-06-10, release date: 2015-12-23, Last modification date: 2024-03-20)

Primary citation

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

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: 26612680
DOI: 10.14348/molcells.2015.0191

Experimental method

X-RAY DIFFRACTION (2.8 Å)