1l1q

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[[Image:1l1q.jpg|left|200px]]<br /><applet load="1l1q" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l1q.jpg|left|200px]]
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caption="1l1q, resolution 1.85&Aring;" />
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'''Crystal Structure of APRTase from Giardia lamblia Complexed with 9-deazaadenine'''<br />
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{{Structure
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|PDB= 1l1q |SIZE=350|CAPTION= <scene name='initialview01'>1l1q</scene>, resolution 1.85&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=9DA:9-DEAZAADENINE'>9DA</scene>
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|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]
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|GENE=
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}}
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'''Crystal Structure of APRTase from Giardia lamblia Complexed with 9-deazaadenine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1L1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Giardia_intestinalis Giardia intestinalis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=9DA:'>9DA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1L1Q OCA].
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1L1Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Giardia_intestinalis Giardia intestinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1Q OCA].
==Reference==
==Reference==
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Closed site complexes of adenine phosphoribosyltransferase from Giardia lamblia reveal a mechanism of ribosyl migration., Shi W, Sarver AE, Wang CC, Tanaka KS, Almo SC, Schramm VL, J Biol Chem. 2002 Oct 18;277(42):39981-8. Epub 2002 Aug 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12171925 12171925]
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Closed site complexes of adenine phosphoribosyltransferase from Giardia lamblia reveal a mechanism of ribosyl migration., Shi W, Sarver AE, Wang CC, Tanaka KS, Almo SC, Schramm VL, J Biol Chem. 2002 Oct 18;277(42):39981-8. Epub 2002 Aug 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12171925 12171925]
[[Category: Adenine phosphoribosyltransferase]]
[[Category: Adenine phosphoribosyltransferase]]
[[Category: Giardia intestinalis]]
[[Category: Giardia intestinalis]]
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[[Category: purine metabolism]]
[[Category: purine metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:25:11 2008''

Revision as of 10:25, 20 March 2008


PDB ID 1l1q

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands: and
Activity: Adenine phosphoribosyltransferase, with EC number 2.4.2.7
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of APRTase from Giardia lamblia Complexed with 9-deazaadenine


Overview

The adenine phosphoribosyltransferase (APRTase) from Giardia lamblia was co-crystallized with 9-deazaadenine and sulfate or with 9-deazaadenine and Mg-phosphoribosylpyrophosphate. The complexes were solved and refined to 1.85 and 1.95 A resolution. Giardia APRTase is a symmetric homodimer with the monomers built around Rossman fold cores, an element common to all known purine phosphoribosyltransferases. The catalytic sites are capped with a small hood domain that is unique to the APRTases. These structures reveal several features relevant to the catalytic function of APRTase: 1) a non-proline cis peptide bond (Glu(61)-Ser(62)) is required to form the pyrophosphate binding site in the APRTase.9dA.MgPRPP complex but is a trans peptide bond in the absence of pyrophosphate group, as observed in the APRTase.9dA.SO4 complex; 2) a catalytic site loop is closed and fully ordered in both complexes, with Glu(100) from the catalytic loop acting as the acid/base for protonation/deprotonation of N-7 of the adenine ring; 3) the pyrophosphoryl charge is neutralized by a single Mg2+ ion and Arg(63), in contrast to the hypoxanthine-guanine phosphoribosyltransferases, which use two Mg2+ ions; and 4) the nearest structural neighbors to APRTases are the orotate phosphoribosyltransferases, suggesting different paths of evolution for adenine relative to other purine PRTases. An overlap comparison of AMP and 9-deazaadenine plus Mg-PRPP at the catalytic sites of APRTases indicated that reaction coordinate motion involves a 2.1-A excursion of the ribosyl anomeric carbon, whereas the adenine ring and the 5-phosphoryl group remained fixed. G. lamblia APRTase therefore provides another example of nucleophilic displacement by electrophile migration.

About this Structure

1L1Q is a Single protein structure of sequence from Giardia intestinalis. Full crystallographic information is available from OCA.

Reference

Closed site complexes of adenine phosphoribosyltransferase from Giardia lamblia reveal a mechanism of ribosyl migration., Shi W, Sarver AE, Wang CC, Tanaka KS, Almo SC, Schramm VL, J Biol Chem. 2002 Oct 18;277(42):39981-8. Epub 2002 Aug 8. PMID:12171925

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