5by2: Difference between revisions
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''' | ==Sedoheptulose 7-phosphate isomerase from Colwellia psychrerythraea strain 34H== | ||
<StructureSection load='5by2' size='340' side='right' caption='[[5by2]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5by2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BY2 FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-sedoheptulose_7-phosphate_isomerase D-sedoheptulose 7-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.28 5.3.1.28] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5by2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5by2 OCA], [http://pdbe.org/5by2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5by2 RCSB], [http://www.ebi.ac.uk/pdbsum/5by2 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/GMHA_COLP3 GMHA_COLP3]] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The psychrophilic organism Colwellia psychrerythraea strain 34H produces extracellular polysaccharide substances to tolerate cold environments. Sedoheptulose 7-phosphate isomerase (GmhA) is essential for producing Dglycero-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 initiatorassociating 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. | |||
Crystal Structure and Comparative Sequence Analysis of GmhA from Colwellia psychrerythraea Strain 34H Provides Insight into Functional Similarity with DiaA.,Do H, Yun JS, Lee CW, Choi YJ, Kim HY, Kim YJ, Park H, Chang JH, Lee JH Mol Cells. 2015 Nov 26. doi: 10.14348/molcells.2015.0191. PMID:26612680<ref>PMID:26612680</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5by2" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: D-sedoheptulose 7-phosphate isomerase]] | |||
[[Category: Chang, J H]] | |||
[[Category: Do, H]] | [[Category: Do, H]] | ||
[[Category: Lee, J | [[Category: Lee, J H]] | ||
[[Category: | [[Category: Yun, J S]] | ||
[[Category: Colwellia psychrerythraea strain 34h]] | |||
[[Category: Cpsgmha]] | |||
[[Category: Isomerase]] | |||
[[Category: Psychrophile]] | |||
[[Category: Sedoheptulose 7-phosphate isomerase]] |
Revision as of 15:39, 23 December 2015
Sedoheptulose 7-phosphate isomerase from Colwellia psychrerythraea strain 34HSedoheptulose 7-phosphate isomerase from Colwellia psychrerythraea strain 34H
Structural highlights
Function[GMHA_COLP3] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. Publication Abstract from PubMedThe psychrophilic organism Colwellia psychrerythraea strain 34H produces extracellular polysaccharide substances to tolerate cold environments. Sedoheptulose 7-phosphate isomerase (GmhA) is essential for producing Dglycero-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 initiatorassociating 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. Crystal Structure and Comparative Sequence Analysis of GmhA from Colwellia psychrerythraea Strain 34H Provides Insight into Functional Similarity with DiaA.,Do H, Yun JS, Lee CW, Choi YJ, Kim HY, Kim YJ, Park H, Chang JH, Lee JH Mol Cells. 2015 Nov 26. doi: 10.14348/molcells.2015.0191. PMID:26612680[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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