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4dfr

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(New page: 200px<br /><applet load="4dfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="4dfr, resolution 1.7&Aring;" /> '''CRYSTAL STRUCTURES OF...)
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[[Image:4dfr.gif|left|200px]]<br /><applet load="4dfr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4dfr, resolution 1.7&Aring;" />
 
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'''CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE==
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X-ray data have been extended to 1.7 A for a binary complex of Escherichia, coli dihydrofolate reductase with methotrexate and a ternary complex of, Lactobacillus casei dihydrofolate reductase with methotrexate and NADPH., Models for both structures have been refined to R factors of 0.15 and, include parameters for fixed and liquid solvent. The two species of, dihydrofolate reductase resemble one another even more closely than was, thought to be the case prior to refinement. Several new structural, features have also been discovered. Among them are a cis peptide linking, Gly-97 and Gly-98 (L. Casei numbering) in both species, an alpha helix, involving residues 43 through 50 in the E. coli enzyme, and the existence, of what may be a specific hydration site on exposed alpha helices., Refinement has led to a revised description of the details of methotrexate, binding. We now see that a fixed water molecule mediates the interaction, between methotrexate's 2-amino group and Thr-116 (L. casei numbering) and, that the inhibitor's 4-amino group makes two hydrogen bonds with the, enzyme (instead of one). Other revisions are also discussed. A, hypothetical model for substrate binding is proposed in which the, pteridine ring is turned upside down while all protein and solvent atoms, remain fixed. Asp-26 in this model is hydrogen bonded to the substrate's, 2-amino group and to N3.
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<StructureSection load='4dfr' size='340' side='right'caption='[[4dfr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4dfr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_B Escherichia coli B]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2dfr 2dfr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DFR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MTX:METHOTREXATE'>MTX</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dfr OCA], [https://pdbe.org/4dfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dfr RCSB], [https://www.ebi.ac.uk/pdbsum/4dfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dfr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/4dfr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=4dfr ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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4DFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_b Escherichia coli b] with CL, CA and MTX as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2DFR. 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=4DFR OCA].
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*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate., Bolin JT, Filman DJ, Matthews DA, Hamlin RC, Kraut J, J Biol Chem. 1982 Nov 25;257(22):13650-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=6815178 6815178]
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[[Category: Escherichia coli B]]
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[[Category: Dihydrofolate reductase]]
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[[Category: Large Structures]]
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[[Category: Escherichia coli b]]
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[[Category: Bolin JT]]
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[[Category: Single protein]]
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[[Category: Filman DJ]]
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[[Category: Bolin, J.T.]]
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[[Category: Kraut J]]
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[[Category: Filman, D.J.]]
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[[Category: Matthews DA]]
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[[Category: Kraut, J.]]
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[[Category: Matthews, D.A.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: MTX]]
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[[Category: oxido-reductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:32:27 2007''
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Current revision

CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE

PDB ID 4dfr

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