1drv

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[[Image:1drv.gif|left|200px]]<br />
 
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<applet load="1drv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1drv, resolution 2.2&Aring;" />
 
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'''ESCHERICHIA COLI DHPR/ACNADH COMPLEX'''<br />
 
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==Overview==
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==ESCHERICHIA COLI DHPR/ACNADH COMPLEX==
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E. coli dihydrodipicolinate reductase exhibits unusual nucleotide, specificity, with NADH being kinetically twice as effective as NADPH as a, reductant as evidenced by their relative V/K values. To investigate the, nature of the interactions which determine this specificity, we performed, isothermal titration calorimetry to determine the thermodynamic parameters, of binding and determined the three-dimensional structures of the, corresponding enzyme-nucleotide complexes. The thermodynamic binding, parameters for NADPH and NADH were determined to be Kd = 2.12 microM, delta G degree = -7.81 kcal mol-1, delta H degree = -10.98 kcal mol-1, and, delta S degree = -10.5 cal mol-1 deg-1 and Kd = 0.46 microM, delta G, degree = -8.74 kcal mol-1, delta H degree = -8.93 kcal mol-1, and delta S, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8873595 (full description)]]
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<StructureSection load='1drv' size='340' side='right'caption='[[1drv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1drv]] 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=1DRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRV FirstGlance]. <br>
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1DRV 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 A3D as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Dihydrodipicolinate_reductase Dihydrodipicolinate reductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.26 1.3.1.26]]. Structure known Active Site: BIN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DRV OCA]].
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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]] 2.2&#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=A3D:3-ACETYLPYRIDINE+ADENINE+DINUCLEOTIDE'>A3D</scene></td></tr>
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==Reference==
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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=1drv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drv OCA], [https://pdbe.org/1drv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1drv RCSB], [https://www.ebi.ac.uk/pdbsum/1drv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1drv ProSAT]</span></td></tr>
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Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes., Reddy SG, Scapin G, Blanchard JS, Biochemistry. 1996 Oct 15;35(41):13294-302. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8873595 8873595]
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</table>
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[[Category: Dihydrodipicolinate reductase]]
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== Function ==
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[https://www.uniprot.org/uniprot/DAPB_ECOLI DAPB_ECOLI] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH.<ref>PMID:7893644</ref> <ref>PMID:20503968</ref>
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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/dr/1drv_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=1drv ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blanchard, J.S.]]
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[[Category: Blanchard JS]]
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[[Category: Reddy, S.G.]]
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[[Category: Reddy SG]]
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[[Category: Scapin, G.]]
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[[Category: Scapin G]]
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[[Category: A3D]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:55:17 2007''
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Current revision

ESCHERICHIA COLI DHPR/ACNADH COMPLEX

PDB ID 1drv

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