1ccj
From Proteopedia
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| - | [[Image:1ccj.jpg|left|200px]]<br /><applet load="1ccj" size=" | + | [[Image:1ccj.jpg|left|200px]]<br /><applet load="1ccj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ccj, resolution 2.1Å" /> | caption="1ccj, resolution 2.1Å" /> | ||
'''CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY'''<br /> | '''CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CCJ 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 HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Known structural/functional Site: <scene name='pdbsite=ACT:Removal Of PHE 202 Forms An Internal Cavity Adjacent To ...'>ACT</scene>. Full crystallographic information is available from [http:// | + | 1CCJ 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=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Known structural/functional Site: <scene name='pdbsite=ACT:Removal+Of+PHE+202+Forms+An+Internal+Cavity+Adjacent+To+...'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:34:31 2008'' |
Revision as of 07:34, 3 February 2008
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CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY
Overview
A large-scale movement between "closed" and "open" conformations of a, protein loop was observed directly with protein crystallography by, trapping individual conformers through binding of an exogenous ligand and, characterization with solution kinetics. The buried indole ring of Trp191, in cytochrome c peroxidase (CCP) was displaced by exogenous ligands, causing a conformational change of loop Pro190-Asn195 and exposing Trp191, to the protein surface. Kinetic measurements are consistent with a, two-step binding mechanism in which the rate-limiting step is a transition, of the protein to the open state, which then binds the ligand. This, large-scale conformational change of a functionally important region of, CCP is independent of ligand and indicates that about 4% of the wild-type, protein is in the open form in solution at any given time.
About this Structure
1CCJ is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Protein conformer selection by ligand binding observed with crystallography., Cao Y, Musah RA, Wilcox SK, Goodin DB, McRee DE, Protein Sci. 1998 Jan;7(1):72-8. PMID:9514261
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