1h3d: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1h3d.png|left|200px]]
-{{STRUCTURE_1h3d|  PDB=1h3d  |  SCENE=  }}
+==STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE==
+<StructureSection load='1h3d' size='340' side='right'caption='[[1h3d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1h3d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3D 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]] 2.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=1h3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3d OCA], [https://pdbe.org/1h3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3d RCSB], [https://www.ebi.ac.uk/pdbsum/1h3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HIS1_ECOLI HIS1_ECOLI] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.[HAMAP-Rule:MF_00079]
+== 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/h3/1h3d_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=1h3d ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+ATP-phosphoribosyltransferase (ATP-PRT), the first enzyme of the histidine pathway, is a complex allosterically regulated enzyme, which controls the flow of intermediates through this biosynthetic pathway. The crystal structures of Escherichia coli ATP-PRT have been solved in complex with the inhibitor AMP at 2.7A and with product PR-ATP at 2.9A (the ribosyl-triphosphate could not be resolved). On the basis of binding of AMP and PR-ATP and comparison with type I PRTs, the PRPP and parts of the ATP-binding site are identified. These structures clearly identify the AMP as binding in the 5-phosphoribosyl-alpha-1-pyrophosphate (PRPP)-binding site, with the adenosine ring occupying the ATP-binding site. Comparison with the recently solved Mycobacterium tuberculosis ATP-PRT structures indicates that histidine is solely responsible for the large conformational changes observed between the hexameric forms of the enzyme. The role of oligomerisation in inhibition and the structural basis for the synergistic inhibition by histidine and AMP are discussed.
-===STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE===
+The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition.,Lohkamp B, McDermott G, Campbell SA, Coggins JR, Lapthorn AJ J Mol Biol. 2004 Feb 6;336(1):131-44. PMID:14741209<ref>PMID:14741209</ref>
-{{ABSTRACT_PUBMED_14741209}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1h3d" style="background-color:#fffaf0;"></div>
-[[1h3d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3D OCA].
 ==See Also==
-*[[ATP Phosphoribosyl Transferase|ATP Phosphoribosyl Transferase]]
+*[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:014741209</ref><references group="xtra"/>
+__TOC__
-[[Category: ATP phosphoribosyltransferase]]
+</StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Escherichia coli K-12]]
-[[Category: Coggins, J R.]]
+[[Category: Large Structures]]
-[[Category: Lapthorn, A J.]]
+[[Category: Coggins JR]]
-[[Category: Lohkamp, B.]]
+[[Category: Lapthorn AJ]]
-[[Category: Mcdermott, G.]]
+[[Category: Lohkamp B]]
-[[Category: Glycosyltransferase]]
+[[Category: McDermott G]]
-[[Category: Hisitidine biosynthesis]]
-[[Category: Phosphoribosyltransferase]]
-[[Category: Transferase]]