1ccj

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[[Image:1ccj.jpg|left|200px]]<br /><applet load="1ccj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ccj.jpg|left|200px]]
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caption="1ccj, resolution 2.1&Aring;" />
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'''CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY'''<br />
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{{Structure
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|PDB= 1ccj |SIZE=350|CAPTION= <scene name='initialview01'>1ccj</scene>, resolution 2.1&Aring;
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|SITE= <scene name='pdbsite=ACT:Removal+Of+PHE+202+Forms+An+Internal+Cavity+Adjacent+To+...'>ACT</scene>
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
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|ACTIVITY= [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]
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|GENE= CCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''CONFORMER SELECTION BY LIGAND BINDING OBSERVED WITH PROTEIN CRYSTALLOGRAPHY'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1CCJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCJ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9514261 9514261]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9514261 9514261]
[[Category: Cytochrome-c peroxidase]]
[[Category: Cytochrome-c peroxidase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: peroxidase]]
[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:46 2008''

Revision as of 08:22, 20 March 2008


PDB ID 1ccj

Drag the structure with the mouse to rotate
, resolution 2.1Å
Sites:
Ligands:
Gene: CCP (Saccharomyces cerevisiae)
Activity: Cytochrome-c peroxidase, with EC number 1.11.1.5
Coordinates: save as pdb, mmCIF, xml



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. 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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