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| | <StructureSection load='1p9n' size='340' side='right'caption='[[1p9n]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1p9n' size='340' side='right'caption='[[1p9n]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1p9n]] is a 2 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=1P9N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P9N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1p9n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P9N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MobB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9n OCA], [https://pdbe.org/1p9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p9n RCSB], [https://www.ebi.ac.uk/pdbsum/1p9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9n ProSAT], [https://www.topsan.org/Proteins/BSGI/1p9n TOPSAN]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9n OCA], [http://pdbe.org/1p9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p9n RCSB], [http://www.ebi.ac.uk/pdbsum/1p9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9n ProSAT], [http://www.topsan.org/Proteins/BSGI/1p9n TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MOBB_ECOLI MOBB_ECOLI]] GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP.<ref>PMID:9219527</ref> <ref>PMID:10978348</ref> <ref>PMID:12682065</ref> | + | [https://www.uniprot.org/uniprot/MOBB_ECOLI MOBB_ECOLI] GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP.<ref>PMID:9219527</ref> <ref>PMID:10978348</ref> <ref>PMID:12682065</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p9/1p9n_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p9/1p9n_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Cygler M]] |
| - | [[Category: Cygler, M]] | + | [[Category: Iannuzzi P]] |
| - | [[Category: Iannuzzi, P]] | + | [[Category: Li Y]] |
| - | [[Category: Li, Y]] | + | [[Category: Matte A]] |
| - | [[Category: Matte, A]] | + | [[Category: Rangarajan SE]] |
| - | [[Category: Rangarajan, S E]] | + | [[Category: Tocilj A]] |
| - | [[Category: Tocilj, A]] | + | |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Mobb]]
| + | |
| - | [[Category: Molybdopterin cofactor biosynthesis]]
| + | |
| Structural highlights
Function
MOBB_ECOLI GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP.[1] [2] [3]
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
The crystal structure of Escherichia coli MobB, an enzyme involved in the final step of molybdenum-cofactor biosynthesis, forms intertwined dimers. Each molecule consists of two segments and requires the second monomer for stable folding. Dimerization buries a quarter of the solvent-accessible area of the monomer. These dimers assemble into a hexagonal lattice with P6(4)22 symmetry and occupy only approximately 25% of the unit-cell volume. The symmetry-related dimers associate tightly into a helical structure with a diameter of 250 A and a pitch of 98 A. Two such helices are intertwined, shifted by 49 A along the sixfold axis. Within the crystal, these helices form thin-walled cylinders with an external diameter of 250 A and an internal diameter of 190 A. Their center is filled with solvent. These cylinders pack closely together, forming a hexagonal lattice with the highest possible packing density. This arrangement of dimers allows extensive intermolecular contacts with 75% solvent content in the crystal.
Molecules of Escherichia coli MobB assemble into densely packed hollow cylinders in a crystal lattice with 75% solvent content.,Rangarajan SE, Tocilj A, Li Y, Iannuzzi P, Matte A, Cygler M Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2348-52. Epub 2003, Nov 27. PMID:14646116[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eaves DJ, Palmer T, Boxer DH. The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein. Eur J Biochem. 1997 Jun 15;246(3):690-7. PMID:9219527
- ↑ 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
- ↑ McLuskey K, Harrison JA, Schuttelkopf AW, Boxer DH, Hunter WN. Insight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structure. J Biol Chem. 2003 Jun 27;278(26):23706-13. Epub 2003 Apr 7. PMID:12682065 doi:10.1074/jbc.M301485200
- ↑ Rangarajan SE, Tocilj A, Li Y, Iannuzzi P, Matte A, Cygler M. Molecules of Escherichia coli MobB assemble into densely packed hollow cylinders in a crystal lattice with 75% solvent content. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2348-52. Epub 2003, Nov 27. PMID:14646116
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