1u9r: Difference between revisions

Revision as of 15:28, 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:1u9r.png

Template:STRUCTURE 1u9r

Crystal Structure of Staphylococcal Nuclease mutant V66E/P117G/H124L/S128A at Room TemperatureCrystal Structure of Staphylococcal Nuclease mutant V66E/P117G/H124L/S128A at Room Temperature

Template:ABSTRACT PUBMED 15377517

About this StructureAbout this Structure

1U9R is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Stabilization of internal charges in a protein: water penetration or conformational change?, Denisov VP, Schlessman JL, Garcia-Moreno E B, Halle B, Biophys J. 2004 Dec;87(6):3982-94. Epub 2004 Sep 17. PMID:15377517

Page seeded by OCA on Mon Jul 28 15:28:12 2008

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

OCA

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-[[Image:1u9r.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1u9r|  PDB=1u9r  |  SCENE=  }}
-'''Crystal Structure of Staphylococcal Nuclease mutant V66E/P117G/H124L/S128A at Room Temperature'''
+===Crystal Structure of Staphylococcal Nuclease mutant V66E/P117G/H124L/S128A at Room Temperature===
-==Overview==
+<!--
-The ionizable amino acid side chains of proteins are usually located at the surface. However, in some proteins an ionizable group is embedded in an apolar internal region. Such buried ionizable groups destabilize the protein and may trigger conformational changes in response to pH variations. Because of the prohibitive energetic cost of transferring a charged group from water to an apolar medium, other stabilizing factors must be invoked, such as ionization-induced water penetration or structural changes. To examine the role of water penetration, we have measured the 17O and 2H magnetic relaxation dispersions (MRD) for the V66E and V66K mutants of staphylococcal nuclease, where glutamic acid and lysine residues are buried in predominantly apolar environments. At neutral pH, where these residues are uncharged, we find no evidence of buried water molecules near the mutation site. This contrasts with a previous cryogenic crystal structure of the V66E mutant, but is consistent with the room-temperature crystal structure reported here. MRD measurements at different pH values show that ionization of Glu-66 or Lys-66 is not accompanied by penetration of long-lived water molecules. On the other hand, the MRD data are consistent with a local conformational change in response to ionization of the internal residues.
+The line below this paragraph, {{ABSTRACT_PUBMED_15377517}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15377517 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15377517}}
 ==About this Structure==
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 [[Category: Nuclease]]
 [[Category: Staphylococcal nuclease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:56:36 2008''
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