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New page: left|200px<br /><applet load="1d1g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d1g, resolution 2.10Å" /> '''DIHYDROFOLATE REDUCT...
 
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[[Image:1d1g.gif|left|200px]]<br /><applet load="1d1g" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1d1g, resolution 2.10&Aring;" />
'''DIHYDROFOLATE REDUCTASE FROM THERMOTOGA MARITIMA'''<br />


==Overview==
==DIHYDROFOLATE REDUCTASE FROM THERMOTOGA MARITIMA==
Two high-resolution structures have been obtained for dihydrofolate, reductase from the hyperthermophilic bacterium Thermotoga maritima in its, unliganded state, and in its ternary complex with the cofactor NADPH and, the inhibitor, methotrexate. While the overall fold of the, hyperthermophilic enzyme is closely similar to monomeric mesophilic, dihydrofolate reductase molecules, its quaternary structure is, exceptional, in that T. maritima dihydrofolate reductase forms a highly, stable homodimer. Here, the molecular reasons for the high intrinsic, stability of the enzyme are elaborated and put in context with the, available data on the physical parameters governing the folding reaction., The molecule is extremely rigid, even with respect to structural changes, during substrate binding and turnover. Subunit cooperativity can be, excluded from structural and biochemical data. Major contributions to the, high intrinsic stability of the enzyme result from the formation of the, dimer. Within the monomer, only subtle stabilizing interactions are, detectable, without clear evidence for any of the typical increments of, thermal stabilization commonly reported for hyperthermophilic proteins., The docking of the subunits is optimized with respect to high packing, density in the dimer interface, additional salt-bridges and beta-sheets., The enzyme does not show significant structural changes upon binding its, coenzyme, NADPH, and the inhibitor, methotrexate. The active-site loop, which is known to play an important role in catalysis in mesophilic, dihydrofolate reductase molecules, is rearranged, participating in the, association of the subunits; it no longer participates in catalysis.
<StructureSection load='1d1g' size='340' side='right'caption='[[1d1g]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D1G 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MTX:METHOTREXATE'>MTX</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=1d1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1g OCA], [https://pdbe.org/1d1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d1g RCSB], [https://www.ebi.ac.uk/pdbsum/1d1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DYR_THEMA DYR_THEMA] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
== 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/d1/1d1g_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=1d1g ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1D1G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with NDP and MTX 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=1D1G OCA].
*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability., Dams T, Auerbach G, Bader G, Jacob U, Ploom T, Huber R, Jaenicke R, J Mol Biol. 2000 Mar 31;297(3):659-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10731419 10731419]
[[Category: Large Structures]]
[[Category: Dihydrofolate reductase]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Auerbach, G.]]
[[Category: Auerbach G]]
[[Category: Bader, G.]]
[[Category: Bader G]]
[[Category: Dams, T.]]
[[Category: Dams T]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Jaenicke, R.]]
[[Category: Jaenicke R]]
[[Category: Ploom, T.]]
[[Category: Ploom T]]
[[Category: MTX]]
[[Category: NDP]]
[[Category: dimer]]
[[Category: hyperthermophile]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:55:41 2007''

Latest revision as of 06:47, 7 February 2024

DIHYDROFOLATE REDUCTASE FROM THERMOTOGA MARITIMA

1d1g, resolution 2.10Å

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