1pzm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:53, 16 August 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_1pzm| PDB=1pzm | SCENE= }}
 
-
===Crystal structure of HGPRT-ase from Leishmania tarentolae in complex with GMP===
 
-
{{ABSTRACT_PUBMED_17894860}}
 
-
==About this Structure==
+
==Crystal structure of HGPRT-ase from Leishmania tarentolae in complex with GMP==
-
[[1pzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leita Leita]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZM OCA].
+
<StructureSection load='1pzm' size='340' side='right'caption='[[1pzm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1pzm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_tarentolae Leishmania tarentolae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PZM FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pzm OCA], [https://pdbe.org/1pzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pzm RCSB], [https://www.ebi.ac.uk/pdbsum/1pzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pzm ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9NJI5_LEITA Q9NJI5_LEITA]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pz/1pzm_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pzm ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
BACKGROUND: Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (EC 2.4.2.8) is a central enzyme in the purine recycling pathway. Parasitic protozoa of the order Kinetoplastida cannot synthesize purines de novo and use the salvage pathway to synthesize purine bases, making this an attractive target for antiparasitic drug design. RESULTS: The glycosomal HGPRT from Leishmania tarentolae in a catalytically active form purified and co-crystallized with a guanosine monophosphate (GMP) in the active site. The dimeric structure of HGPRT has been solved by molecular replacement and refined against data extending to 2.1 A resolution. The structure reveals the contacts of the active site residues with GMP. CONCLUSION: Comparative analysis of the active sites of Leishmania and human HGPRT revealed subtle differences in the position of the ligand and its interaction with the active site residues, which could be responsible for the different reactivities of the enzymes to allopurinol reported in the literature. The solution and analysis of the structure of Leishmania HGPRT may contribute to further investigations leading to a full understanding of this important enzyme family in protozoan parasites.
-
==See Also==
+
Crystal structure of Leishmania tarentolae hypoxanthine-guanine phosphoribosyltransferase.,Monzani PS, Trapani S, Thiemann OH, Oliva G BMC Struct Biol. 2007 Sep 25;7:59. PMID:17894860<ref>PMID:17894860</ref>
-
*[[Phosphoribosyltransferase|Phosphoribosyltransferase]]
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:017894860</ref><references group="xtra"/><references/>
+
</div>
-
[[Category: Hypoxanthine phosphoribosyltransferase]]
+
<div class="pdbe-citations 1pzm" style="background-color:#fffaf0;"></div>
-
[[Category: Leita]]
+
 
-
[[Category: Monzani, P S.]]
+
==See Also==
-
[[Category: Oliva, G.]]
+
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
-
[[Category: Thiemann, O H.]]
+
== References ==
-
[[Category: Trapani, S.]]
+
<references/>
-
[[Category: Transferase]]
+
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Leishmania tarentolae]]
 +
[[Category: Monzani PS]]
 +
[[Category: Oliva G]]
 +
[[Category: Thiemann OH]]
 +
[[Category: Trapani S]]

Current revision

Crystal structure of HGPRT-ase from Leishmania tarentolae in complex with GMP

PDB ID 1pzm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pzm"
Personal tools