4ue3

From Proteopedia

(Difference between revisions)

Revision as of 08:42, 21 May 2019

The Mechanism of Hydrogen Activation by NiFe-hydrogenases and the Importance of the active site Arginine

Structural highlights

4ue3 is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , ,
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 Using hydrogenase-1 from Escherichia coli, the strictly conserved residues R509 and D574 have been replaced by lysine (R509K) and asparagine (D574N) and the highly conserved D118 has been replaced by alanine (D118A) or asparagine (D118N/D574N).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/4ue3"

@@ Line 1: / Line 1: @@
 ==The Mechanism of Hydrogen Activation by NiFe-hydrogenases and the Importance of the active site Arginine==
-<StructureSection load='4ue3' size='340' side='right' caption='[[4ue3]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+<StructureSection load='4ue3' size='340' side='right'caption='[[4ue3]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ue3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UE3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ue3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UE3 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NFV:NI-FE+OXIDIZED+ACTIVE+CENTER'>NFV</scene>, <scene name='pdbligand=SF3:FE4-S3+CLUSTER'>SF3</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4ue3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ue3 OCA], [http://pdbe.org/4ue3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ue3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ue3 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=4ue3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ue3 OCA], [http://pdbe.org/4ue3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ue3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ue3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ue3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Armstrong, F A]]
 [[Category: Carr, S B]]

4ue3

From Proteopedia

Revision as of 08:42, 21 May 2019

The Mechanism of Hydrogen Activation by NiFe-hydrogenases and the Importance of the active site Arginine

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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