1h4d: Difference between revisions

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<StructureSection load='1h4d' size='340' side='right'caption='[[1h4d]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
<StructureSection load='1h4d' size='340' side='right'caption='[[1h4d]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1h4d]] is a 1 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=1H4D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H4D FirstGlance]. <br>
<table><tr><td colspan='2'>[[1h4d]] is a 1 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=1H4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4D FirstGlance]. <br>
</td></tr><tr id='ligand'><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></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]] 1.74&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e5k|1e5k]], [[1fr9|1fr9]], [[1frw|1frw]], [[1h4c|1h4c]], [[1h4e|1h4e]], [[1hjj|1hjj]], [[1hjl|1hjl]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene></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=1h4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4d OCA], [http://pdbe.org/1h4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h4d RCSB], [http://www.ebi.ac.uk/pdbsum/1h4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4d ProSAT]</span></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=1h4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4d OCA], [https://pdbe.org/1h4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4d RCSB], [https://www.ebi.ac.uk/pdbsum/1h4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[https://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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Buchanan, G]]
[[Category: Buchanan G]]
[[Category: Guse, A]]
[[Category: Guse A]]
[[Category: Kuper, J]]
[[Category: Kuper J]]
[[Category: Lawson, D M]]
[[Category: Lawson DM]]
[[Category: Mendel, R R]]
[[Category: Mendel RR]]
[[Category: Palmer, T]]
[[Category: Palmer T]]
[[Category: Schwarz, G]]
[[Category: Schwarz G]]
[[Category: Stevenson, C E.M]]
[[Category: Stevenson CEM]]
[[Category: Gtp-binding]]
[[Category: Molybdenum cofactor biosynthesis]]
[[Category: Molybdopterin nucleotidyl-transferase]]
Retrieved from "https://proteopedia.org/1h4d"