1h4e: Difference between revisions

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[[Image:1h4e.png|left|200px]]
==BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA==
<StructureSection load='1h4e' size='340' side='right' caption='[[1h4e]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1h4e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H4E FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e5k|1e5k]], [[1fr9|1fr9]], [[1frw|1frw]], [[1h4c|1h4c]], [[1h4d|1h4d]], [[1hjj|1hjj]], [[1hjl|1hjl]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h4e RCSB], [http://www.ebi.ac.uk/pdbsum/1h4e PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h4/1h4e_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


{{STRUCTURE_1h4e|  PDB=1h4e  |  SCENE=  }}
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<ref>PMID:12719427</ref>


===BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_12719427}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1h4e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4E OCA].
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Buchanan, G.]]
[[Category: Buchanan, G.]]

Revision as of 15:34, 28 September 2014

BIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBABIOCHEMICAL AND STRUCTURAL ANALYSIS OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA

Structural highlights

1h4e 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, 1h4d, 1hjj, 1hjl
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

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

References

  1. ↑ 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

1h4e, resolution 1.65Å

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