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5a4f

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Revision as of 08:45, 14 November 2018

The mechanism of Hydrogen Activation by NiFe-hydrogenases.

Structural highlights

5a4f is a 4 chain structure with sequence from Escherichia coli str. k-12 substr. mc4100. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , ,
NonStd Res:
Related:	5a4i, 5a4m
Gene:	hyaB, b0973, JW0955 (Escherichia coli str. K-12 substr. MC4100), hyaA, b0972, JW0954 (Escherichia coli str. K-12 substr. MC4100)
Activity:	Hydrogenase (acceptor), with EC number 1.12.99.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MBHL_ECOLI] This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. [MBHS_ECOLI] This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.

Publication Abstract from PubMed

The active site of [NiFe] hydrogenases contains a strictly conserved arginine that suspends a guanidine nitrogen atom <4.5 A above the nickel and iron atoms. The guanidine headgroup interacts with the side chains of two conserved aspartic acid residues to complete an outer-shell canopy that has thus far proved intractable to investigation by site-directed mutagenesis. Using hydrogenase-1 from Escherichia coli, the strictly conserved residues R509 and D574 have been replaced by lysine (R509K) and asparagine (D574N) and the highly conserved D118 has been replaced by alanine (D118A) or asparagine (D118N/D574N). Each enzyme variant is stable, and their [(RS)2Nimu(SR)2Fe(CO)(CN)2] inner coordination shells are virtually unchanged. The R509K variant had >100-fold lower activity than native enzyme. Conversely, the variants D574N, D118A and D118N/D574N, in which the position of the guanidine headgroup is retained, showed 83%, 26% and 20% activity, respectively. The special kinetic requirement for R509 implicates the suspended guanidine group as the general base in H2 activation by [NiFe] hydrogenases.

Mechanism of hydrogen activation by [NiFe] hydrogenases.,Evans RM, Brooke EJ, Wehlin SA, Nomerotskaia E, Sargent F, Carr SB, Phillips SE, Armstrong FA Nat Chem Biol. 2015 Nov 30. doi: 10.1038/nchembio.1976. PMID:26619250^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Evans RM, Brooke EJ, Wehlin SA, Nomerotskaia E, Sargent F, Carr SB, Phillips SE, Armstrong FA. Mechanism of hydrogen activation by [NiFe] hydrogenases. Nat Chem Biol. 2015 Nov 30. doi: 10.1038/nchembio.1976. PMID:26619250 doi:http://dx.doi.org/10.1038/nchembio.1976

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5a4f"

@@ Line 1: / Line 1: @@
 ==The mechanism of Hydrogen Activation by NiFe-hydrogenases.==
 <StructureSection load='5a4f' size='340' side='right' caption='[[5a4f]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a4i|5a4i]], [[5a4m|5a4m]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hyaB, b0973, JW0955 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1403831 Escherichia coli str. K-12 substr. MC4100]), hyaA, b0972, JW0954 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1403831 Escherichia coli str. K-12 substr. MC4100])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogenase_(acceptor) Hydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.99.6 1.12.99.6] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a4f OCA], [http://pdbe.org/5a4f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a4f RCSB], [http://www.ebi.ac.uk/pdbsum/5a4f PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a4f OCA], [http://pdbe.org/5a4f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a4f RCSB], [http://www.ebi.ac.uk/pdbsum/5a4f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a4f ProSAT]</span></td></tr>
 </table>
 == Function ==

5a4f

From Proteopedia

Revision as of 08:45, 14 November 2018

The mechanism of Hydrogen Activation by NiFe-hydrogenases.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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