We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2anb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2anb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2anb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2anb| PDB=2anb | SCENE= }}
{{STRUCTURE_2anb| PDB=2anb | SCENE= }}
-
'''Crystal Structure Of Oligomeric E.coli Guanylate Kinase In Complex With GMP'''
+
===Crystal Structure Of Oligomeric E.coli Guanylate Kinase In Complex With GMP===
-
==Overview==
+
<!--
-
Guanosine monophosphate kinases (GMPKs), which catalyze the phosphorylation of GMP and dGMP to their diphosphate form, have been characterized as monomeric enzymes in eukaryotes and prokaryotes. Here, we report that GMPK from Escherichia coli (ecGMPK) assembles in solution and in the crystal as several different oligomers. Thermodynamic analysis of ecGMPK using differential scanning calorimetry shows that the enzyme is in equilibrium between a dimer and higher order oligomers, whose relative amounts depend on protein concentration, ionic strength, and the presence of ATP. Crystallographic structures of ecGMPK in the apo, GMP and GDP-bound forms were solved at 3.2A, 2.9A and 2.4A resolution, respectively. ecGMPK forms a hexamer with D3 symmetry in all crystal forms, in which the two nucleotide-binding domains are able to undergo closure comparable to that of monomeric GMPKs. The 2-fold and 3-fold interfaces involve a 20-residue C-terminal extension and a sequence signature, respectively, that are missing from monomeric eukaryotic GMPKs, explaining why ecGMPK forms oligomers. These signatures are found in GMPKs from proteobacteria, some of which are human pathogens. GMPKs from these bacteria are thus likely to form the same quaternary structures. The shift of the thermodynamic equilibrium towards the dimer at low ecGMPK concentration together with the observation that inter-subunit interactions partially occlude the ATP-binding site in the hexameric structure suggest that the dimer may be the active species at physiological enzyme concentration.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16140325}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16140325 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16140325}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Oligomeric]]
[[Category: Oligomeric]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:14:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:52:06 2008''

Revision as of 12:52, 27 July 2008

Image:2anb.png

Template:STRUCTURE 2anb

Crystal Structure Of Oligomeric E.coli Guanylate Kinase In Complex With GMP

Template:ABSTRACT PUBMED 16140325

About this Structure

2ANB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase., Hible G, Renault L, Schaeffer F, Christova P, Zoe Radulescu A, Evrin C, Gilles AM, Cherfils J, J Mol Biol. 2005 Oct 7;352(5):1044-59. PMID:16140325

Page seeded by OCA on Sun Jul 27 15:52:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2anb"
Personal tools