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2g37

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(New page: 200px<br /><applet load="2g37" size="350" color="white" frame="true" align="right" spinBox="true" caption="2g37, resolution 2.000&Aring;" /> '''Structure of Thermu...)
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[[Image:2g37.gif|left|200px]]<br /><applet load="2g37" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2g37, resolution 2.000&Aring;" />
 
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'''Structure of Thermus thermophilus L-proline dehydrogenase'''<br />
 
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==Overview==
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==Structure of Thermus thermophilus L-proline dehydrogenase==
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Proline dehydrogenase (PRODH) and pyrroline-5-carboxylate dehydrogenase, (P5CDH) catalyze the two-step oxidation of proline to glutamate. They are, distinct monofunctional enzymes in all eukaryotes and some bacteria, but, are fused into bifunctional enzymes known as Proline utilization A (PutA), in other bacteria. Here we report the first structure and biochemical data, for a monofunctional PRODH. The 2.0 A resolution structure of Thermus, thermophilus PRODH reveals a distorted (betaalpha)(8) barrel catalytic, core domain and a hydrophobic alpha-helical domain located above the, carboxyl terminal ends of the strands of the barrel. Although the, catalytic core is similar to that of the PutA PRODH domain, the FAD, conformation of T. thermophilus PRODH is remarkably different and likely, reflects unique requirements for membrane association and communication, with P5CDH. Also, the FAD of T. thermophilus PRODH is highly solvent, exposed compared to PutA due to a 4-A shift of helix 8. Structure-based, sequence analysis of the PutA/PRODH family led us to identify 9 conserved, motifs involved in cofactor and substrate recognition. Biochemical studies, show that the midpoint potential of the FAD is -75 mV and the kinetic, parameters for proline are K(m)=27 mM and k(cat)=13 s (-1)., 3,4-dehydro-L-proline was found to be an efficient substrate and, L-tetrahydro-2-furoic acid is a competitive inhibitor (K(I)=1.0 mM)., Finally, we demonstrate that PRODH reacts with O(2) producing superoxide., This is significant because superoxide production underlies the role of, human PRODH in p53-mediated apoptosis, implying commonalities between, eukaryotic and bacterial monofunctional PRODHs.
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<StructureSection load='2g37' size='340' side='right'caption='[[2g37]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2g37]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G37 FirstGlance]. <br>
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2G37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Proline_dehydrogenase Proline dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.8 1.5.99.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G37 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&#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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=2g37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g37 OCA], [https://pdbe.org/2g37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g37 RCSB], [https://www.ebi.ac.uk/pdbsum/2g37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g37 ProSAT]</span></td></tr>
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Structure and kinetics of monofunctional proline dehydrogenase from thermus thermophilus., White TA, Krishnan N, Becker DF, Tanner JJ, J Biol Chem. 2007 Mar 7;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17344208 17344208]
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</table>
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[[Category: Proline dehydrogenase]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/PRODH_THET2 PRODH_THET2] Converts proline to delta-1-pyrroline-5-carboxylate (PubMed:17344208, PubMed:18426222). Has significant activity against O(2) producing superoxide during proline oxidation catalytic cycle (PubMed:17344208).<ref>PMID:17344208</ref> <ref>PMID:18426222</ref>
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[[Category: Thermus thermophilus]]
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== Evolutionary Conservation ==
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[[Category: Tanner, J.J.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: White, T.A.]]
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Check<jmol>
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[[Category: FAD]]
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<jmolCheckbox>
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[[Category: MPD]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/2g37_consurf.spt"</scriptWhenChecked>
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[[Category: beta8-alpha8-barrel]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: flavoenzyme]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:03:03 2008''
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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=2g37 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>
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus HB27]]
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[[Category: Tanner JJ]]
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[[Category: White TA]]

Current revision

Structure of Thermus thermophilus L-proline dehydrogenase

PDB ID 2g37

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