2ypi
From Proteopedia
(New page: 200px<br /> <applet load="2ypi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ypi, resolution 2.5Å" /> '''CRYSTALLOGRAPHIC ANA...) |
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caption="2ypi, resolution 2.5Å" /> | caption="2ypi, resolution 2.5Å" /> | ||
'''CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE AND 2-PHOSPHOGLYCOLATE AT 2.5-ANGSTROMS RESOLUTION. IMPLICATIONS FOR CATALYSIS'''<br /> | '''CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE AND 2-PHOSPHOGLYCOLATE AT 2.5-ANGSTROMS RESOLUTION. IMPLICATIONS FOR CATALYSIS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2YPI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PGA as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 2YPI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http:// | + | 2YPI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PGA:'>PGA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 2YPI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YPI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: triose phosphate isomerase]] | [[Category: triose phosphate isomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:42:44 2008'' |
Revision as of 15:42, 15 February 2008
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CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE AND 2-PHOSPHOGLYCOLATE AT 2.5-ANGSTROMS RESOLUTION. IMPLICATIONS FOR CATALYSIS
Overview
The binding of the transition-state analogue 2-phosphoglycolate to, triosephosphate isomerase from yeast has been investigated, crystallographically. An atomic model of the enzyme-inhibitor complex has, been refined against data to 2.5-A resolution to a final R factor of 0.18., The interactions between the inhibitor and enzyme have been analyzed. The, inhibitor forms hydrogen bonds to the side chains of His 95 and Glu 165., The latter hydrogen bond confirms that Glu 165 is protonated upon PGA, binding. The structure of the complexed enzyme has been compared to that, of the unbound form of the enzyme, and conformational changes have been, observed: the side chain of Glu 165 moves over 2 A and a 10-residue, flexible loop moves over 7 A to close over the active site. Spectroscopic, results of phosphoglycolic acid binding to triosephosphate isomerase that, have been amassed over the years are also explained in structural terms., The implications for catalysis are noted.
About this Structure
2YPI is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. The following page contains interesting information on the relation of 2YPI with [The Glycolytic Enzymes]. Active as Triose-phosphate isomerase, with EC number 5.3.1.1 Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis., Lolis E, Petsko GA, Biochemistry. 1990 Jul 17;29(28):6619-25. PMID:2204418
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