1eq0: Difference between revisions

Revision as of 01:36, 1 July 2008

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File:1eq0.png

Template:STRUCTURE 1eq0

SOLUTION STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE COMPLEXED WITH MGAMPPCPSOLUTION STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE COMPLEXED WITH MGAMPPCP

Template:ABSTRACT PUBMED 11546767

About this StructureAbout this Structure

1EQ0 is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

Unusual conformational changes in 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as revealed by X-ray crystallography and NMR., Xiao B, Shi G, Gao J, Blaszczyk J, Liu Q, Ji X, Yan H, J Biol Chem. 2001 Oct 26;276(43):40274-81. Epub 2001 Aug 23. PMID:11546767

Page seeded by OCA on Tue Jul 1 01:36:28 2008

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

OCA

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-[[Image:1eq0.gif|left|200px]]
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 {{STRUCTURE_1eq0|  PDB=1eq0  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE COMPLEXED WITH MGAMPPCP'''
+===SOLUTION STRUCTURE OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE COMPLEXED WITH MGAMPPCP===
-==Overview==
+<!--
-The crystal structure of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) in complex with MgADP has been determined at 1.5-A resolution with a crystallographic R factor of 0.191. The solution structure of HPPK in complex with Mg(2+) and beta,gamma-methyleneadenosine 5'-triphosphate (MgAMPPCP) has been determined using a simulated annealing protocol with 3,523 experimental NMR restraints. The root mean square deviation of the ensemble of 20 refined conformers that represent the solution structure from the mean coordinate set derived from them is 0.74 +/- 0.26 A for all backbone atoms and 0.49 +/- 0.22 A when residues Pro(14), Pro(44)-Gln(50), and Arg(84)-Pro(91) are excluded. Binding of MgADP causes significant changes in the conformation and dynamical property of three loops of HPPK that are involved in catalysis. A dramatic, unusual conformational change is that loop 3 moves away from the active center significantly with some residues moving by &gt;17 A. The binding of MgADP also stabilizes loop 1 and loop 3 but makes loop 2 more mobile. Very similar conformational and dynamical changes are observed in the NMR solution structure of HPPK.MgAMPPCP. The conformational and dynamical changes may play important roles in both substrate binding and product release in the catalytic cycle.
+The line below this paragraph, {{ABSTRACT_PUBMED_11546767}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11546767 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11546767}}
 ==About this Structure==
-EQ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ0 OCA].
+EQ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ0 OCA].
 ==Reference==
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 [[Category: Pyrophosphokinase]]
 [[Category: Pyrophosphoryl transfer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:23:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:36:28 2008''