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[[Image:1fdi.gif|left|200px]]<br />
<applet load="1fdi" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fdi, resolution 2.9&Aring;" />
'''OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI COMPLEXED WITH THE INHIBITOR NITRITE'''<br />


==Overview==
==OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI COMPLEXED WITH THE INHIBITOR NITRITE==
Formate dehydrogenase H from Escherichia coli contains selenocysteine, (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD), cofactors, and an Fe4S4 cluster at the active site and catalyzes the, two-electron oxidation of formate to carbon dioxide. The crystal, structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate, dehydrogenase H (with and without bound inhibitor) and the reduced, [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain, alphabeta structure with the molybdenum directly coordinated to selenium, and both MGD cofactors. These structures suggest a reaction mechanism that, directly involves SeCys140 and His141 in proton abstraction and the, molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron, transfer.
<StructureSection load='1fdi' size='340' side='right'caption='[[1fdi]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fdi]] 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=1FDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FDI 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=1fdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdi OCA], [https://pdbe.org/1fdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fdi RCSB], [https://www.ebi.ac.uk/pdbsum/1fdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FDHF_ECOLI FDHF_ECOLI] Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors.
== 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/fd/1fdi_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=1fdi ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FDI 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 NO2, SF4, MGD and 6MO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2]]. Structure known Active Sites: FS4 and MO4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FDI OCA]].
*[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster., Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD, Science. 1997 Feb 28;275(5304):1305-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9036855 9036855]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Formate dehydrogenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Boyington JC]]
[[Category: Boyington, J.C.]]
[[Category: Sun PD]]
[[Category: Sun, P.D.]]
[[Category: 6MO]]
[[Category: MGD]]
[[Category: NO2]]
[[Category: SF4]]
[[Category: anaerobic]]
[[Category: dehydrogenase]]
[[Category: fe4s4]]
[[Category: formate]]
[[Category: iron sulfur cluster]]
[[Category: mgd]]
[[Category: molybdenum]]
[[Category: molybdopterin]]
[[Category: molybdopterin guanine dinucleotide]]
[[Category: mpt]]
[[Category: oxidoreductase]]
[[Category: secys]]
[[Category: selenium]]
[[Category: selenocysteine]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:11:54 2007''

Latest revision as of 10:13, 7 February 2024

OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI COMPLEXED WITH THE INHIBITOR NITRITEOXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI COMPLEXED WITH THE INHIBITOR NITRITE

Structural highlights

1fdi is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FDHF_ECOLI Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1fdi, resolution 2.90Å

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