This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1e2w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1e2w.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1e2w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e2w| PDB=1e2w | SCENE= }}
{{STRUCTURE_1e2w| PDB=1e2w | SCENE= }}
-
'''N168F MUTANT OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII'''
+
===N168F MUTANT OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10924110}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10924110 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10924110}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Internal water chain]]
[[Category: Internal water chain]]
[[Category: Photosynthetic function impaired]]
[[Category: Photosynthetic function impaired]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:35:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:03:28 2008''

Revision as of 21:03, 30 June 2008

Image:1e2w.png

Template:STRUCTURE 1e2w

N168F MUTANT OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII

Template:ABSTRACT PUBMED 10924110

About this Structure

1E2W is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 1 00:03:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e2w"
Personal tools