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3ir6

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Revision as of 08:12, 1 November 2017

Crystal structure of NarGHI mutant NarG-H49S

Structural highlights

3ir6 is a 3 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
NonStd Res:
Related:	1q16, 3ir5, 3ir7
Gene:	narG, bisD, narC, b1224, JW1215 (ECOLI), narH, b1225, JW1216 (ECOLI), narI, chlI, b1227, JW1218 (ECOLI)
Activity:	Nitrate reductase, with EC number 1.7.99.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NARG_ECOLI] The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction. [NARI_ECOLI] The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. [NARH_ECOLI] The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.

Evolutionary Conservation

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

Publication Abstract from PubMed

We have used site-directed mutagenesis, EPR spectroscopy, redox potentiometry, and protein crystallography to monitor assembly of the FS0 [4Fe-4S] cluster and molybdo-bis(pyranopterin guanine dinucleotide) cofactor (Mo-bisPGD) of the Escherichia coli nitrate reductase A (NarGHI) catalytic subunit (NarG). Cys and Ser mutants of NarG-His(49) both lack catalytic activity, with only the former assembling FS0 and Mo-bisPGD. Importantly, both prosthetic groups are absent in the NarG-H49S mutant. EPR spectroscopy of the Cys mutant reveals that the E(m) value of the FS0 cluster is decreased by at least 500 mV, preventing its participation in electron transfer to the Mo-bisPGD cofactor. To demonstrate that decreasing the FS0 cluster E(m) results in decreased enzyme activity, we mutated a critical Arg residue (NarG-Arg(94)) in the vicinity of FS0 to a Ser residue. In this case, the E(m) of FS0 is decreased by 115 mV, with a concomitant decrease in enzyme turnover to approximately 30% of the wild type. Analysis of the structure of the NarG-H49S mutant reveals two important aspects of NarGHI maturation: (i) apomolybdo-NarGHI is able to bind GDP moieties at their respective P and Q sites in the absence of the Mo-bisPGD cofactor, and (ii) a critical segment of residues in NarG, (49)HGVNCTG(55), must be correctly positioned to ensure holoenzyme maturation.

Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation.,Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990^[1]

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

References

↑ Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ir6"

@@ Line 1: / Line 1: @@
 ==Crystal structure of NarGHI mutant NarG-H49S==
 <StructureSection load='3ir6' size='340' side='right' caption='[[3ir6]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 8: / Line 9: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">narG, bisD, narC, b1224, JW1215 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), narH, b1225, JW1216 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), narI, chlI, b1227, JW1218 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrate_reductase Nitrate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.4 1.7.99.4] </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=3ir6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ir6 OCA], [http://pdbe.org/3ir6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ir6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ir6 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=3ir6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ir6 OCA], [http://pdbe.org/3ir6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ir6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ir6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ir6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 31: / Line 32: @@
 </div>
 <div class="pdbe-citations 3ir6" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Nitrate reductase|Nitrate reductase]]
 == References ==
 <references/>
@@ Line 44: / Line 42: @@
 [[Category: Strynadka, N C.J]]
 [[Category: Weiner, J H]]
+[[Category: 3fe-4]]
+[[Category: 4fe-4]]
 [[Category: Cell inner membrane]]
 [[Category: Cell membrane]]

3ir6

From Proteopedia

Revision as of 08:12, 1 November 2017

Crystal structure of NarGHI mutant NarG-H49S

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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