1g2q: Difference between revisions

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[[Image:1g2q.jpg|left|200px]]<br /><applet load="1g2q" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1g2q.jpg|left|200px]]
caption="1g2q, resolution 1.50&Aring;" />
 
'''CRYSTAL STRUCTURE OF ADENINE PHOSPHORIBOSYLTRANSFERASE'''<br />
{{Structure
|PDB= 1g2q |SIZE=350|CAPTION= <scene name='initialview01'>1g2q</scene>, resolution 1.50&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7]
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF ADENINE PHOSPHORIBOSYLTRANSFERASE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1G2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Adenine_phosphoribosyltransferase Adenine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.7 2.4.2.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2Q OCA].  
1G2Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2Q OCA].  


==Reference==
==Reference==
Structural analysis of adenine phosphoribosyltransferase from Saccharomyces cerevisiae., Shi W, Tanaka KS, Crother TR, Taylor MW, Almo SC, Schramm VL, Biochemistry. 2001 Sep 11;40(36):10800-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11535055 11535055]
Structural analysis of adenine phosphoribosyltransferase from Saccharomyces cerevisiae., Shi W, Tanaka KS, Crother TR, Taylor MW, Almo SC, Schramm VL, Biochemistry. 2001 Sep 11;40(36):10800-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11535055 11535055]
[[Category: Adenine phosphoribosyltransferase]]
[[Category: Adenine phosphoribosyltransferase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: single domain]]
[[Category: single domain]]


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Revision as of 12:17, 20 March 2008

File:1g2q.jpg


PDB ID 1g2q

Drag the structure with the mouse to rotate
, resolution 1.50Å
Activity: Adenine phosphoribosyltransferase, with EC number 2.4.2.7
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF ADENINE PHOSPHORIBOSYLTRANSFERASE


OverviewOverview

Adenine phosphoribosyltransferase (APRTase) is a widely distributed enzyme, and its deficiency in humans causes the accumulation of 2,8-dihydroxyadenine. It is the sole catalyst for adenine recycling in most eukaryotes. The most commonly expressed APRTase has subunits of approximately 187 amino acids, but the only crystal structure is from Leishmania donovani, which expresses a long form of the enzyme with 237 residues. Saccharomyces cerevisiae APRTase was selected as a representative of the short APRTases, and the structure of the apo-enzyme and sulfate bound forms were solved to 1.5 and 1.75 A, respectively. Yeast APRTase is a dimeric molecule, and each subunit is composed of a central five-stranded beta-sheet surrounded by five alpha-helices, a structural theme found in all known purine phosphoribosyltransferases. The structures reveal several important features of APRTase function: (i) sulfate ions bound at the 5'-phosphate and pyrophosphate binding sites; (ii) a nonproline cis peptide bond (Glu67-Ser68) at the pyrophosphate binding site in both apo-enzyme and sulfate-bound forms; and (iii) a catalytic loop that is open and ordered in the apo-enzyme but open and disordered in the sulfate-bound form. Alignment of conserved amino acids in short-APRTases from 33 species reveals 13 invariant and 15 highly conserved residues present in hinges, catalytic site loops, and the catalytic pocket. Mutagenesis of conserved residues in the catalytic loop, subunit interface, and phosphoribosylpyrophosphate binding site indicates critical roles for the tip of the catalytic loop (Glu106) and a catalytic site residue Arg69, respectively. Mutation of one loop residue (Tyr103Phe) increases k(cat) by 4-fold, implicating altered dynamics for the catalytic site loop.

About this StructureAbout this Structure

1G2Q is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of adenine phosphoribosyltransferase from Saccharomyces cerevisiae., Shi W, Tanaka KS, Crother TR, Taylor MW, Almo SC, Schramm VL, Biochemistry. 2001 Sep 11;40(36):10800-9. PMID:11535055

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