1zn9: Difference between revisions

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 [[Image:1zn9.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1zn9 |SIZE=350|CAPTION= <scene name='initialview01'>1zn9</scene>, resolution 2.05&Aring;
+The line below this paragraph, containing "STRUCTURE_1zn9", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE= APRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+-->
-|DOMAIN=
+{{STRUCTURE_1zn9|  PDB=1zn9  |  SCENE=  }}
-|RELATEDENTRY=[[1ore|1ORE]], [[1zn7|1ZN7]], [[1zn8|1ZN8]]
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zn9 OCA], [http://www.ebi.ac.uk/pdbsum/1zn9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zn9 RCSB]</span>
-}}
 '''Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms'''
+==Overview==
+Adenine phosphoribosyltransferase (APRT) is an important enzyme component of the purine recycling pathway. Parasitic protozoa of the order Kinetoplastida are unable to synthesize purines de novo and use the salvage pathway for the synthesis of purine bases rendering this biosynthetic pathway an attractive target for antiparasitic drug design. The recombinant human adenine phosphoribosyltransferase (hAPRT) structure was resolved in the presence of AMP in the active site to 1.76 A resolution and with the substrates PRPP and adenine simultaneously bound to the catalytic site to 1.83 A resolution. An additional structure was solved containing one subunit of the dimer in the apo-form to 2.10 A resolution. Comparisons of these three hAPRT structures with other 'type I' PRTases revealed several important features of this class of enzymes. Our data indicate that the flexible loop structure adopts an open conformation before and after binding of both substrates adenine and PRPP. Comparative analyses presented here provide structural evidence to propose the role of Glu104 as the residue that abstracts the proton of adenine N9 atom before its nucleophilic attack on the PRPP anomeric carbon. This work leads to new insights to the understanding of the APRT catalytic mechanism.
 ==Disease==
@@ Line 20: / Line 20: @@
 ==About this Structure==
 ZN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZN9 OCA].
+==Reference==
+Structural Complexes of Human Adenine Phosphoribosyltransferase Reveal Novel Features of the APRT Catalytic Mechanism., Silva CH, Silva M, Iulek J, Thiemann OH, J Biomol Struct Dyn. 2008 Jun;25(6):589-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18399692 18399692]
 [[Category: Adenine phosphoribosyltransferase]]
 [[Category: Homo sapiens]]
@@ Line 27: / Line 30: @@
 [[Category: Thiemann, O H.]]
 [[Category: Tomich, C H.T P.]]
-[[Category: glycosyltransferase]]
+[[Category: Glycosyltransferase]]
-[[Category: polymorphism]]
+[[Category: Polymorphism]]
-[[Category: purine salvage]]
+[[Category: Purine salvage]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:23:42 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:39:05 2008''