6dfr: Difference between revisions

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OCA

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-[[Image:6dfr.gif|left|200px]]<br /><applet load="6dfr" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="6dfr, resolution 2.4&Aring;" />
-'''CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE'''<br />
-==Overview==
+==CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE==
-The crystal structure of dihydrofolate reductase (EC 1.5.1.3) from, Escherichia coli has been solved as the binary complex with NADP+ (the, holoenzyme) and as the ternary complex with NADP+ and folate. The Bragg, law resolutions of the structures are 2.4 and 2.5 A, respectively. The new, crystal forms are nonisomorphous with each other and with the methotrexate, binary complex reported earlier [Bolin, J. T., Filman, D. J., Matthews, D., A., Hamlin, R. C., &amp; Kraut, J. (1982) J. Biol. Chem. 257, 13650-13662]. In, general, NADP+ and folate binding conform to predictions, but the, nicotinamide moiety of NADP+ is disordered in the holoenzyme and ordered, in the ternary complex. A mobile loop (residues 16-20) involved in binding, the nicotinamide is also disordered in the holoenzyme. We report a, detailed analysis of the binding interactions for both ligands, paying, special attention to several apparently strained interactions that may, favor the transition state for hydride transfer. Hypothetical models are, presented for the binding of 7,8-dihydrofolate in the Michaelis complex, and for the transition-state complex.
+<StructureSection load='6dfr' size='340' side='right'caption='[[6dfr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6dfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DFR 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]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=6dfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dfr OCA], [https://pdbe.org/6dfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dfr RCSB], [https://www.ebi.ac.uk/pdbsum/6dfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dfr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
+== 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/df/6dfr_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=6dfr ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-DFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CA and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=6DFR OCA].
+*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state., Bystroff C, Oatley SJ, Kraut J, Biochemistry. 1990 Apr 3;29(13):3263-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2185835 2185835]
-[[Category: Dihydrofolate reductase]]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bystroff, C.]]
+[[Category: Bystroff C]]
-[[Category: Kraut, J.]]
+[[Category: Kraut J]]
-[[Category: Oatley, S.J.]]
+[[Category: Oatley SJ]]
-[[Category: CA]]
-[[Category: NAP]]
-[[Category: oxido-reductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:31:40 2007''