3f47

From Proteopedia

(Difference between revisions)

Revision as of 22:13, 24 December 2014

The Crystal Structure of [Fe]-Hydrogenase (Hmd) Holoenzyme from Methanocaldococcus jannaschii

Structural highlights

3f47 is a 1 chain structure with sequence from Methanocaldococcus jannaschii. The March 2009 RCSB PDB Molecule of the Month feature on Hydrogenase by David Goodsell is 10.2210/rcsb_pdb/mom_2009_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	2b0j, 3dag, 3daf, 3f46
Gene:	hmd, MJ0784 (Methanocaldococcus jannaschii)
Activity:	5,10-methenyltetrahydromethanopterin hydrogenase, with EC number 1.12.98.2
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[HMD_METJA] Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT (By similarity).

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

[Fe]-hydrogenase is one of three types of enzymes known to activate H(2). Crystal structure analysis recently revealed that its active site iron is ligated square-pyramidally by Cys176-sulfur, two CO, an "unknown" ligand and the sp(2)-hybridized nitrogen of a unique iron-guanylylpyridinol-cofactor. We report here on the structure of the C176A mutated enzyme crystallized in the presence of dithiothreitol (DTT). It suggests an iron center octahedrally coordinated by one DTT-sulfur and one DTT-oxygen, two CO, the 2-pyridinol's nitrogen and the 2-pyridinol's 6-formylmethyl group in an acyl-iron ligation. This result led to a re-interpretation of the iron ligation in the wild-type.

The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex.,Hiromoto T, Ataka K, Pilak O, Vogt S, Stagni MS, Meyer-Klaucke W, Warkentin E, Thauer RK, Shima S, Ermler U FEBS Lett. 2009 Feb 4;583(3):585-90. Epub 2009 Jan 20. PMID:19162018^[1]

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

References

↑ Hiromoto T, Ataka K, Pilak O, Vogt S, Stagni MS, Meyer-Klaucke W, Warkentin E, Thauer RK, Shima S, Ermler U. The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. FEBS Lett. 2009 Feb 4;583(3):585-90. Epub 2009 Jan 20. PMID:19162018 doi:http://dx.doi.org/10.1016/j.febslet.2009.01.017

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3f47"

@@ Line 9: / Line 9: @@
 <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=3f47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f47 RCSB], [http://www.ebi.ac.uk/pdbsum/3f47 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/HMD_METJA HMD_METJA]] Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3f47

From Proteopedia

Revision as of 22:13, 24 December 2014

The Crystal Structure of [Fe]-Hydrogenase (Hmd) Holoenzyme from Methanocaldococcus jannaschii

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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