1bq4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1bq4.gif|left|200px]]
{{Seed}}
[[Image:1bq4.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bq4|  PDB=1bq4  |  SCENE=  }}  
{{STRUCTURE_1bq4|  PDB=1bq4  |  SCENE=  }}  


'''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH BENZENE HEXACARBOXYLATE'''
===SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH BENZENE HEXACARBOXYLATE===




==Overview==
<!--
The effects that the inhibitors inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates have on the phosphoglycerate mutases from Saccharomyces cerevisiae and Schizosaccharomyces pombe have been determined. Their Kivalues have been calculated, and the ability of the inhibitors to protect the enzymes against limited proteolysis investigated. These biochemical data have been placed in a structural context by the solution of the crystal structures of S. cerevisiae phosphoglycerate mutase soaked with inositol hexakisphosphate or benzene hexacarboxylate. These large polyanionic compounds bind to the enzyme so as to block the entrance to the active-site cleft. They form multiple interactions with the enzyme, consistent with their low Kivalues, and afford good protection against limited proteolysis of the C-terminal region by thermolysin. The inositol compound is more efficacious because of its greater number of negative charges. The S. pombe phosphoglycerate mutase that is inherently lacking a comparable C-terminal region has higher Kivalues for the compounds tested. Moreover, the S. pombe enzyme is less sensititive to proteolysis, and the presence or absence of the inhibitor molecules has little effect on susceptibility to proteolysis.
The line below this paragraph, {{ABSTRACT_PUBMED_10369755}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10369755 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10369755}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Glycolytic enzyme]]
[[Category: Glycolytic enzyme]]
[[Category: Isomerase]]
[[Category: Isomerase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:49:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:31:18 2008''

Revision as of 16:31, 30 June 2008

File:1bq4.png

Template:STRUCTURE 1bq4

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH BENZENE HEXACARBOXYLATE

Template:ABSTRACT PUBMED 10369755

About this Structure

1BQ4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis., Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA, J Mol Biol. 1999 Jun 18;289(4):691-9. PMID:10369755

Page seeded by OCA on Mon Jun 30 19:31:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1bq4&oldid=578939"