1e2v: Difference between revisions

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[[Image:1e2v.gif|left|200px]]<br />
[[Image:1e2v.gif|left|200px]]<br /><applet load="1e2v" size="450" color="white" frame="true" align="right" spinBox="true"  
<applet load="1e2v" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1e2v, resolution 1.85&Aring;" />
caption="1e2v, resolution 1.85&Aring;" />
'''N153Q MUTANT OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII'''<br />
'''N153Q MUTANT OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII'''<br />
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==About this Structure==
==About this Structure==
1E2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with ACT and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5 and AC6. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E2V OCA].  
1E2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with ACT and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Hec Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Hec Binding Site For Chain B'>AC2</scene>, <scene name='pdbsite=AC3:Hec Binding Site For Chain C Symmetry Related Subunits C ...'>AC3</scene>, <scene name='pdbsite=AC4:Act Binding Site For Chain A Symmetry Related Subunits C ...'>AC4</scene>, <scene name='pdbsite=AC5:Act Binding Site For Chain A Symmetry Related Subunits C ...'>AC5</scene> and <scene name='pdbsite=AC6:Act Binding Site For Chain B Symmetry Related Subunits C ...'>AC6</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E2V OCA].  


==Reference==
==Reference==
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[[Category: photosynthetic function impaired]]
[[Category: photosynthetic function impaired]]


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Revision as of 15:42, 18 December 2007

File:1e2v.gif


1e2v, resolution 1.85Å

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N153Q MUTANT OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII

OverviewOverview

The structure of cytochrome f includes an internal chain of five water, molecules and six hydrogen-bonding side chains, which are conserved, throughout the phylogenetic range of photosynthetic organisms from higher, plants, algae, and cyanobacteria. The in vivo electron transfer capability, of Chlamydomonas reinhardtii cytochrome f was impaired in site-directed, mutants of the conserved Asn and Gln residues that form hydrogen bonds, with water molecules of the internal chain [Ponamarev, M. V., and Cramer, W. A. (1998) Biochemistry 37, 17199-17208]. The 251-residue extrinsic, functional domain of C. reinhardtii cytochrome f was expressed in, Escherichia coli without the 35 C-terminal residues of the intact, cytochrome that contain the membrane anchor. Crystal structures were, determined for the wild type and three "water chain" mutants (N168F, Q158L, and N153Q) having impaired photosynthetic and electron transfer, function. The mutant cytochromes were produced, folded, and assembled heme, at levels identical to that of the wild type in the E. coli expression, system. N168F, which had a non-photosynthetic phenotype and was thus most, affected by mutational substitution, also had the greatest structural, perturbation with two water molecules (W4 and W5) displaced from the, internal chain. Q158L, the photosynthetic mutant with the largest, impairment of in vivo electron transfer, had a more weakly bound water at, one position (W1). N153Q, a less impaired photosynthetic mutant, had an, internal water chain with positions and hydrogen bonds identical to those, of the wild type. The structure data imply that the waters of the internal, chain, in addition to the surrounding protein, have a significant role in, cytochrome f function.

About this StructureAbout this Structure

1E2V is a Single protein structure of sequence from Chlamydomonas reinhardtii with ACT and HEC as ligands. Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.

ReferenceReference

Interruption of the internal water chain of cytochrome f impairs photosynthetic function., Sainz G, Carrell CJ, Ponamarev MV, Soriano GM, Cramer WA, Smith JL, Biochemistry. 2000 Aug 8;39(31):9164-73. PMID:10924110

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