Document Detail


Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop.
MedLine Citation:
PMID:  8451239     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Two mutants of adenylate kinase from Escherichia coli have been crystallized and analyzed by X-ray diffraction at resolutions of 3.4 and 2.4 A, respectively. These mutants are Pro-9-->Leu and Gly-10-->Val. They were selected for their positions in the highly conserved Gly-loop forming a giant anion hole for the beta-phosphate of ATP (GTP) in adenylate kinases, H-ras-p21, and other nucleotide-binding proteins. Mutants at these positions of H-ras-p21 cause cancer. In adenylate kinase these mutations cause smallish changes at the active site. Relating the structural changes to the known changes in catalysis indicates that these mutants hinder the induced-fit movements. As a side result we find that mutant Pro-9-->Leu and wild-type form one very similar crystal packing contact that is crystallographic in one case and noncrystallographic in the other, while all other packing contacts and the space groups are quite at variance.
Authors:
C W Müller; G E Schulz
Related Documents :
21741359 - Toward the smallest active subdomain of a tim-barrel fold: insights from a truncated α-...
20008249 - Therapeutic potential of jak2 inhibitors.
21878319 - Kinetic, mutagenic, and structural homology analysis of l-serine dehydratase from legio...
14757059 - Crystal structure of a camp-dependent protein kinase mutant at 1.26a: new insights into...
21549129 - Unexpected active-site flexibility in the structure of human neutrophil elastase in com...
21656889 - Fine tuning of a biological machine: dnak gains improved chaperone activity by altered ...
9480879 - Intergenic suppression of the gammam23k uncoupling mutation in f0f1 atp synthase by bet...
8910559 - Immobilization of the c-terminal extension of bovine alphaa-crystallin reduces chaperon...
1350309 - Selective beta 3-adrenergic agonists of brown adipose tissue and thermogenesis. 1. [4-[...
Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Proteins     Volume:  15     ISSN:  0887-3585     ISO Abbreviation:  Proteins     Publication Date:  1993 Jan 
Date Detail:
Created Date:  1993-04-14     Completed Date:  1993-04-14     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  42-9     Citation Subset:  IM    
Affiliation:
Institut für Organische Chemie und Biochemie der Universität, Freiburg im Breisgau, Federal Republic of Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adenylate Kinase / chemistry*,  isolation & purification
Carrier Proteins / chemistry
Crystallization
Cyclic AMP Receptor Protein*
Escherichia coli / enzymology*
Models, Chemical
Models, Molecular
Mutation
Protein Conformation
Proto-Oncogene Proteins p21(ras) / chemistry
Receptors, Cyclic AMP / chemistry
X-Ray Diffraction
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Cyclic AMP Receptor Protein; 0/Receptors, Cyclic AMP; EC 2.7.4.3/Adenylate Kinase; EC 3.6.5.2/Proto-Oncogene Proteins p21(ras)

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Characterization of proline-containing alpha-helix (helix F model of bacteriorhodopsin) by molecular...
Next Document:  Thermodynamic integration calculations of binding free energy difference for Gly-169 mutation in sub...