1qk3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qk3.gif|left|200px]]<br /><applet load="1qk3" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1qk3.gif|left|200px]]
-
caption="1qk3, resolution 1.65&Aring;" />
+
 
-
'''TOXOPLASMA GONDII HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE GMP COMPLEX'''<br />
+
{{Structure
 +
|PDB= 1qk3 |SIZE=350|CAPTION= <scene name='initialview01'>1qk3</scene>, resolution 1.65&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=5GP:GUANOSINE-5'-MONOPHOSPHATE'>5GP</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Hypoxanthine_phosphoribosyltransferase Hypoxanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.8 2.4.2.8]
 +
|GENE=
 +
}}
 +
 
 +
'''TOXOPLASMA GONDII HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE GMP COMPLEX'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1QK3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii] with <scene name='pdbligand=5GP:'>5GP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hypoxanthine_phosphoribosyltransferase Hypoxanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.8 2.4.2.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QK3 OCA].
+
1QK3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QK3 OCA].
==Reference==
==Reference==
-
Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex., Heroux A, White EL, Ross LJ, Borhani DW, Biochemistry. 1999 Nov 2;38(44):14485-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10545170 10545170]
+
Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex., Heroux A, White EL, Ross LJ, Borhani DW, Biochemistry. 1999 Nov 2;38(44):14485-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10545170 10545170]
[[Category: Hypoxanthine phosphoribosyltransferase]]
[[Category: Hypoxanthine phosphoribosyltransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 23: Line 32:
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:30 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:38:39 2008''

Revision as of 11:38, 20 March 2008


PDB ID 1qk3

Drag the structure with the mouse to rotate
, resolution 1.65Å
Ligands:
Activity: Hypoxanthine phosphoribosyltransferase, with EC number 2.4.2.8
Coordinates: save as pdb, mmCIF, xml



TOXOPLASMA GONDII HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE GMP COMPLEX


Overview

The crystal structures of the guanosine 5'-monophosphate (GMP) and inosine 5'-monophosphate (IMP) complexes of Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase (HGPRT) have been determined at 1.65 and 1.90 A resolution. These complexes, which crystallize in space groups P2(1) (a = 65.45 A, b = 90.84 A, c = 80. 26 A, and beta = 92.53 degrees ) and P2(1)2(1)2(1) (a = 84.54 A, b = 102.44 A, and c = 108.83 A), each comprise a tetramer in the crystallographic asymmetric unit. All active sites in the tetramers are fully occupied by the nucleotide. Comparison of these structures with that of the xanthosine 5'-monophosphate (XMP)-pyrophosphate-Mg(2+) ternary complex reported in the following article [Heroux, A., et al. (1999) Biochemistry 38, 14495-14506] shows how T. gondii HGPRT is able to recognize guanine, hypoxanthine, and xanthine as substrates, and suggests why the human enzyme cannot use xanthine efficiently. Comparison with the apoenzyme reveals the structural changes that occur upon binding of purines and ribose 5'-phosphate to HGPRT. Two structural features important to the HGPRT mechanism, a previously unrecognized active site loop (loop III', residues 180-184) and an active site peptide bond (Leu78-Lys79) that adopts both the cis and the trans configurations, are presented.

About this Structure

1QK3 is a Single protein structure of sequence from Toxoplasma gondii. Full crystallographic information is available from OCA.

Reference

Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex., Heroux A, White EL, Ross LJ, Borhani DW, Biochemistry. 1999 Nov 2;38(44):14485-94. PMID:10545170

Page seeded by OCA on Thu Mar 20 13:38:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools