1hpu: Difference between revisions

Revision as of 08:30, 1 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:1hpu.png

Template:STRUCTURE 1hpu

5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP

Template:ABSTRACT PUBMED 11491293

About this StructureAbout this Structure

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

ReferenceReference

Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures., Knofel T, Strater N, J Mol Biol. 2001 May 25;309(1):239-54. PMID:11491293

Page seeded by OCA on Tue Jul 1 08:30:48 2008

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OCA

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-[[Image:1hpu.gif|left|200px]]
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 {{STRUCTURE_1hpu|  PDB=1hpu  |  SCENE=  }}
-'''5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP'''
+===5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP===
-==Overview==
+<!--
-'-Nucleotidase belongs to a large superfamily of distantly related dinuclear metallophosphatases including the Ser/Thr protein phosphatases and purple acid phosphatases. The protein undergoes a 96 degrees domain rotation between an open (inactive) and a closed (active) enzyme form. Complex structures of the closed form with the products adenosine and phosphate, and with the substrate analogue inhibitor alpha,beta-methylene ADP, have been determined at 2.1 A and 1.85 A resolution, respectively. In addition, a complex of the open form of 5'-nucleotidase with ATP was analyzed at a resolution of 1.7 A. These structures show that the adenosine group binds to a specific binding pocket of the C-terminal domain. The adenine ring is stacked between Phe429 and Phe498. The N-terminal domain provides the ligands to the dimetal cluster and the conserved His117, which together form the catalytic core structure. However, the three C-terminal arginine residues 375, 379 and 410, which are involved in substrate binding, may also play a role in transition-state stabilization. The beta-phosphate group of the inhibitor is terminally coordinated to the site 2 metal ion. The site 1 metal ion coordinates a water molecule which is in an ideal position for a nucleophilic attack on the phosphorus atom, assuming an in-line mechanism of phosphoryl transfer. Another water molecule bridges the two metal ions.
+The line below this paragraph, {{ABSTRACT_PUBMED_11491293}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11491293 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11491293}}
 ==About this Structure==
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 [[Category: Metalloenzyme]]
 [[Category: Metallophosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:06:07 2008''
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