1e5k: Difference between revisions
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<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=1e5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e5k RCSB], [http://www.ebi.ac.uk/pdbsum/1e5k PDBsum]</span></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=1e5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e5k RCSB], [http://www.ebi.ac.uk/pdbsum/1e5k PDBsum]</span></td></tr> | ||
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||