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1h4d

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Revision as of 16:24, 25 December 2014

BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA

Structural highlights

1h4d 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.
Ligands:	,
Related:	1e5k, 1fr9, 1frw, 1h4c, 1h4e, 1hjj, 1hjl
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[MOBA_ECOLI] Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP can not be utilized.^[1] ^[2] ^[3] ^[4]

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

Molybdopterin guanine dinucleotide (MGD) is the form of the molybdenum cofactor that is required for the activity of most bacterial molybdoenzymes. MGD is synthesized from molybdopterin (MPT) and GTP in a reaction catalyzed by the MobA protein. Here we report that wild type MobA can be copurified along with bound MPT and MGD, demonstrating a tight binding of both its substrate and product. To study structure-function relationships, we have constructed a number of site-specific mutations of the most highly conserved amino acid residues of the MobA protein family. Variant MobA proteins were characterized for their ability to support the synthesis of active molybdenum enzymes, to bind MPT and MGD, to interact with the molybdenum cofactor biosynthesis proteins MobB and MoeA. They were also characterized by x-ray structural analysis. Our results suggest an essential role for glycine 15 of MobA, either for GTP binding and/or catalysis, and an involvement of glycine 82 in the stabilization of the product-bound form of the enzyme. Surprisingly, the individual and double substitution of asparagines 180 and 182 to aspartate did not affect MPT binding, catalysis, and product stabilization.

Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA.,Guse A, Stevenson CE, Kuper J, Buchanan G, Schwarz G, Giordano G, Magalon A, Mendel RR, Lawson DM, Palmer T J Biol Chem. 2003 Jul 11;278(28):25302-7. Epub 2003 Apr 28. PMID:12719427^[5]

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

References

↑ Palmer T, Vasishta A, Whitty PW, Boxer DH. Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli. Eur J Biochem. 1994 Jun 1;222(2):687-92. PMID:8020507
↑ Johnson JL, Indermaur LW, Rajagopalan KV. Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide. J Biol Chem. 1991 Jul 5;266(19):12140-5. PMID:1648082
↑ Temple CA, Rajagopalan KV. Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J Biol Chem. 2000 Dec 22;275(51):40202-10. PMID:10978348 doi:http://dx.doi.org/10.1074/jbc.M007407200
↑ Neumann M, Seduk F, Iobbi-Nivol C, Leimkuhler S. Molybdopterin dinucleotide biosynthesis in Escherichia coli: identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides. J Biol Chem. 2011 Jan 14;286(2):1400-8. doi: 10.1074/jbc.M110.155671. Epub 2010, Nov 16. PMID:21081498 doi:http://dx.doi.org/10.1074/jbc.M110.155671
↑ Guse A, Stevenson CE, Kuper J, Buchanan G, Schwarz G, Giordano G, Magalon A, Mendel RR, Lawson DM, Palmer T. Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA. J Biol Chem. 2003 Jul 11;278(28):25302-7. Epub 2003 Apr 28. PMID:12719427 doi:http://dx.doi.org/10.1074/jbc.M302639200

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/1h4d"

@@ Line 7: / Line 7: @@
 <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=1h4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h4d RCSB], [http://www.ebi.ac.uk/pdbsum/1h4d PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MOBA_ECOLI MOBA_ECOLI]] Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP can not be utilized.<ref>PMID:8020507</ref> <ref>PMID:1648082</ref> <ref>PMID:10978348</ref> <ref>PMID:21081498</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1h4d

From Proteopedia

Revision as of 16:24, 25 December 2014

BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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