1c8s

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{{STRUCTURE_1c8s| PDB=1c8s | SCENE= }}
{{STRUCTURE_1c8s| PDB=1c8s | SCENE= }}
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'''BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE'''
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===BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE===
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==Overview==
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Crystal structures of the Asp96 to Asn mutant of the light-driven proton pump bacteriorhodopsin and its M photointermediate produced by illumination at ambient temperature have been determined to 1.8 and 2.0 angstroms resolution, respectively. The trapped photoproduct corresponds to the late M state in the transport cycle-that is, after proton transfer to Asp85 and release of a proton to the extracellular membrane surface, but before reprotonation of the deprotonated retinal Schiff base. Its density map describes displacements of side chains near the retinal induced by its photoisomerization to 13-cis,15-anti and an extensive rearrangement of the three-dimensional network of hydrogen-bonded residues and bound water that accounts for the changed pKa values (where Ka is the acid constant) of the Schiff base and Asp85. The structural changes detected suggest the means for conserving energy at the active site and for ensuring the directionality of proton translocation.
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(as it appears on PubMed at http://www.pubmed.gov), where 10514362 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10514362}}
==About this Structure==
==About this Structure==
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[[Category: Photoreceptor]]
[[Category: Photoreceptor]]
[[Category: Retinal protein]]
[[Category: Retinal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:28:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:22:34 2008''

Revision as of 17:22, 30 June 2008

Image:1c8s.png

Template:STRUCTURE 1c8s

BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE

Template:ABSTRACT PUBMED 10514362

About this Structure

1C8S is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.

Reference

Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution., Luecke H, Schobert B, Richter HT, Cartailler JP, Lanyi JK, Science. 1999 Oct 8;286(5438):255-61. PMID:10514362

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