1zxh: Difference between revisions

Revision as of 01:42, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zxh.png

Template:STRUCTURE 1zxh

G311 mutant proteinG311 mutant protein

Template:ABSTRACT PUBMED 16245921

About this StructureAbout this Structure

1ZXH is a Single protein structure of sequence from Streptococcus sp.. Full experimental information is available from OCA.

ReferenceReference

Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds., He Y, Yeh DC, Alexander P, Bryan PN, Orban J, Biochemistry. 2005 Nov 1;44(43):14055-61. PMID:16245921

Page seeded by OCA on Tue Jul 29 01:42:25 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1zxh|  PDB=1zxh  |  SCENE=  }}
-'''G311 mutant protein'''
+===G311 mutant protein===
-==Overview==
+<!--
-We describe here the solution NMR structures of two IgG binding domains with highly homologous sequences but different three-dimensional structures. The proteins, G311 and A219, are derived from the IgG binding domains of their wild-type counterparts, protein G and protein A, respectively. Through a series of site-directed mutations and phage display selections, the sequences of G311 and A219 were designed to converge to a point of high-level sequence identity while keeping their respective wild-type tertiary folds. Structures of both artificially evolved sequences were determined by NMR spectroscopy. The main chain fold of G311 can be superimposed on the wild-type alpha/beta protein G structure with a backbone rmsd of 1.4 A, and the A219 structure can be overlaid on the wild-type three-alpha-helix protein A fold also with a backbone rmsd of 1.4 A. The structure of G311, in particular, accommodates a large number of mutational changes without undergoing a change in the overall fold of the main chain. The structural differences are maintained despite a high level (59%) of sequence identity. These proteins serve as starting points for further experiments that will probe basic concepts of protein folding and conformational switching.
+The line below this paragraph, {{ABSTRACT_PUBMED_16245921}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16245921 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16245921}}
 ==About this Structure==
-ZXH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXH OCA].
+ZXH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXH OCA].
 ==Reference==
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 [[Category: Phage display]]
 [[Category: Protein g]]
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