1mne: Difference between revisions

Revision as of 00:27, 3 July 2008

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File:1mne.png

Template:STRUCTURE 1mne

TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATETRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE

Template:ABSTRACT PUBMED 7619796

About this StructureAbout this Structure

1MNE is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution., Smith CA, Rayment I, Biochemistry. 1995 Jul 18;34(28):8973-81. PMID:7619796

Page seeded by OCA on Thu Jul 3 00:27:50 2008

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

OCA

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 {{STRUCTURE_1mne|  PDB=1mne  |  SCENE=  }}
-'''TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE'''
+===TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE===
-==Overview==
+<!--
-The structure of the magnesium pyrophosphate complex of the truncated head of Dictyostelium myosin has been determined by molecular replacement at 2.7 A resolution and refined to a crystallographic R-factor of 16.0%. The crystals belong to the orthorhombic space group P2(1)2(1)2, where a = 105.2 A, b = 182.1 A, and c = 54.5 A. The conformation of the protein around the magnesium pyrophosphate is very similar to that seen when magnesium ADP-beryllium fluoride binds in the active site. The latter complex mimics the binding of ATP prior to hydrolysis. The pyrophosphate molecule occupies the beta- and gamma-phosphate sites, where the two phosphorus atoms are in the same positions as the beta-phosphate and the BeFx moiety of the beryllium fluoride-trapped ADP. The surrounding active site residues are almost perfectly superimposable in the two structures and the hydrogen-bonding interactions that the PPi makes with the protein are essentially identical. The similarity between the MgPPi and MgADP.BeFx complex with S1Dc suggests that the conformational change, which occurs when ATP binds to actomyosin and which reduces the affinity of myosin for actin, is caused by the binding of the gamma- and beta-phosphate groups of the nucleotide. This then implies that the role of the remainder of the substrate is to increase the binding affinity for myosin and thus to drive the equilibrium toward dissociation of myosin from actin.
+The line below this paragraph, {{ABSTRACT_PUBMED_7619796}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7619796 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7619796}}
 ==About this Structure==
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 [[Category: Myosin]]
 [[Category: Phosphorylation]]
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