2ou9: Difference between revisions

Revision as of 07:04, 28 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:2ou9.png

Template:STRUCTURE 2ou9

Structure of Spin-labeled T4 Lysozyme Mutant T115R1/R119AStructure of Spin-labeled T4 Lysozyme Mutant T115R1/R119A

Template:ABSTRACT PUBMED 17473014

About this StructureAbout this Structure

2OU9 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme., Guo Z, Cascio D, Hideg K, Kalai T, Hubbell WL, Protein Sci. 2007 Jun;16(6):1069-86. Epub 2007 May 1. PMID:17473014

Page seeded by OCA on Mon Jul 28 07:04:49 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ou9.gif|left|200px]]
+{{Seed}}
+[[Image:2ou9.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2ou9|  PDB=2ou9  |  SCENE=  }}
-'''Structure of Spin-labeled T4 Lysozyme Mutant T115R1/R119A'''
+===Structure of Spin-labeled T4 Lysozyme Mutant T115R1/R119A===
-==Overview==
+<!--
-A nitroxide side chain (R1) has been substituted at single sites along a helix-turn-helix motif in T4 lysozyme (residues 114-135). Together with previously published data, the new sites reported complete a continuous scan through the motif. Mutants with R1 at sites 115 and 118 were selected for crystallographic analysis to identify the structural origins of the corresponding two-component EPR spectra. At 115, R1 is shown to occupy two rotamers in the room temperature crystal structure, one of which has not been previously reported. The two components in the EPR spectrum apparently arise from differential interactions of the two rotamers with the surrounding structure, the most important of which is a hydrophobic interaction of the nitroxide ring. Interestingly, the crystal structure at 100 K reveals a single rotamer, emphasizing the possibility of rotamer selection in low-temperature crystal structures. Residue 118 is at a solvent-inaccessible site in the protein core, and the structure of 118R1, the first reported for the R1 side chain at a buried site, reveals how the side chain is accommodated in an overpacked core.
+The line below this paragraph, {{ABSTRACT_PUBMED_17473014}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17473014 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17473014}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Spin label]]
 [[Category: T4 lysozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:40:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:04:49 2008''