1q5i

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q5i.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1q5i.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q5i| PDB=1q5i | SCENE= }}
{{STRUCTURE_1q5i| PDB=1q5i | SCENE= }}
-
'''Crystal structure of bacteriorhodopsin mutant P186A crystallized from bicelles'''
+
===Crystal structure of bacteriorhodopsin mutant P186A crystallized from bicelles===
-
==Overview==
+
<!--
-
One of the hallmarks of membrane protein structure is the high frequency of transmembrane helix kinks, which commonly occur at proline residues. Because the proline side chain usually precludes normal helix geometry, it is reasonable to expect that proline residues generate these kinks. We observe, however, that the three prolines in bacteriorhodopsin transmembrane helices can be changed to alanine with little structural consequences. This finding leads to a conundrum: if proline is not required for helix bending, why are prolines commonly present at bends in transmembrane helices? We propose an evolutionary hypothesis in which a mutation to proline initially induces the kink. The resulting packing defects are later repaired by further mutation, thereby locking the kink in the structure. Thus, most prolines in extant proteins can be removed without major structural consequences. We further propose that nonproline kinks are places where vestigial prolines were later removed during evolution. Consistent with this hypothesis, at 14 of 17 nonproline kinks in membrane proteins of known structure, we find prolines in homologous sequences. Our analysis allows us to predict kink positions with &gt;90% reliability. Kink prediction indicates that different G protein-coupled receptor proteins have different kink patterns and therefore different structures.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14732697}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14732697 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14732697}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alpha helix]]
[[Category: Alpha helix]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:53:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:10:30 2008''

Revision as of 10:10, 29 July 2008

Template:STRUCTURE 1q5i

Crystal structure of bacteriorhodopsin mutant P186A crystallized from bicelles

Template:ABSTRACT PUBMED 14732697

About this Structure

1Q5I is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.

Reference

The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors., Yohannan S, Faham S, Yang D, Whitelegge JP, Bowie JU, Proc Natl Acad Sci U S A. 2004 Jan 27;101(4):959-63. Epub 2004 Jan 19. PMID:14732697

Page seeded by OCA on Tue Jul 29 13:10:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools