1dqr: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1dqr.gif|left|200px]]
{{Seed}}
[[Image:1dqr.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dqr|  PDB=1dqr  |  SCENE=  }}  
{{STRUCTURE_1dqr|  PDB=1dqr  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR'''
===CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR===




==Overview==
<!--
The multifunctional protein phosphoglucose isomerase, also known as neuroleukin, autocrine motility factor, and differentiation and maturation mediator, has different roles inside and outside the cell. In the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine. We have determined the three-dimensional structure of rabbit muscle phosphoglucose isomerase complexed with the competitive inhibitor D-gluconate 6-phosphate by X-ray crystallography at 2.5 A resolution. The structure shows that the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit. The location of the bound D-gluconate 6-phosphate inhibitor leads to the identification of residues involved in substrate specificity (Ser209, Ser159, Thr214, Thr217, and Thr211). The results of previously published kinetic studies suggest that a lysine and a histidine are involved in the catalytic mechanism. The crystal structure suggests active site residues Lys518 and His388 might be these residues. In addition, the positions of amino acid residues that are substituted in the genetic disease nonspherocytic hemolytic anemia suggest how these substitutions can result in altered catalysis or protein stability.
The line below this paragraph, {{ABSTRACT_PUBMED_10653639}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10653639 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10653639}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Anti-parallel beta sheet]]
[[Category: Anti-parallel beta sheet]]
[[Category: Parallel beta sheet]]
[[Category: Parallel beta sheet]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:09:49 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:28:42 2008''

Revision as of 20:28, 30 June 2008

File:1dqr.png

Template:STRUCTURE 1dqr

CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR

Template:ABSTRACT PUBMED 10653639

About this Structure

1DQR is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator., Jeffery CJ, Bahnson BJ, Chien W, Ringe D, Petsko GA, Biochemistry. 2000 Feb 8;39(5):955-64. PMID:10653639

Page seeded by OCA on Mon Jun 30 23:28:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1dqr&oldid=588689"