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{{STRUCTURE_4ap8|  PDB=4ap8  |  SCENE=  }}
===Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B)===


==Disease==
==Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B)==
[[http://www.uniprot.org/uniprot/MOC2B_HUMAN MOC2B_HUMAN]] Molybdenum cofactor deficiency type B (MOCOD type B) [MIM:[http://omim.org/entry/252150 252150]]: Autosomal recessive disease which leads to the pleiotropic loss of all molybdoenzyme activities and is characterized by severe neurological damage, neonatal seizures and early childhood death. Note=The disease is caused by mutations affecting the gene represented in this entry.  
<StructureSection load='4ap8' size='340' side='right'caption='[[4ap8]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
 
== Structural highlights ==
==Function==
<table><tr><td colspan='2'>[[4ap8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AP8 FirstGlance]. <br>
[[http://www.uniprot.org/uniprot/MOC2B_HUMAN MOC2B_HUMAN]] Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.<ref>PMID:12732628</ref> <ref>PMID:15073332</ref>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.78&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ap8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ap8 OCA], [https://pdbe.org/4ap8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ap8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ap8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ap8 ProSAT]</span></td></tr>
[[4ap8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AP8 OCA].
</table>
 
== Disease ==
==Reference==
[https://www.uniprot.org/uniprot/MOC2B_HUMAN MOC2B_HUMAN] Molybdenum cofactor deficiency type B (MOCOD type B) [MIM:[https://omim.org/entry/252150 252150]: Autosomal recessive disease which leads to the pleiotropic loss of all molybdoenzyme activities and is characterized by severe neurological damage, neonatal seizures and early childhood death. Note=The disease is caused by mutations affecting the gene represented in this entry.
<references group="xtra"/><references/>
== Function ==
[https://www.uniprot.org/uniprot/MOC2B_HUMAN MOC2B_HUMAN] Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.<ref>PMID:12732628</ref> <ref>PMID:15073332</ref>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Molybdopterin synthase]]
[[Category: Large Structures]]
[[Category: Allerston, C.]]
[[Category: Allerston C]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C.]]
[[Category: Bountra C]]
[[Category: Burgess-Brown, N.]]
[[Category: Burgess-Brown N]]
[[Category: Delft, F von.]]
[[Category: Edwards A]]
[[Category: Edwards, A.]]
[[Category: Froese DS]]
[[Category: Froese, D S.]]
[[Category: Goubin S]]
[[Category: Goubin, S.]]
[[Category: Kiyani W]]
[[Category: Kiyani, W.]]
[[Category: Krojer T]]
[[Category: Krojer, T.]]
[[Category: Vollmar M]]
[[Category: Vollmar, M.]]
[[Category: Yue WW]]
[[Category: Yue, W W.]]
[[Category: Von Delft F]]
[[Category: Transferase]]

Latest revision as of 14:32, 20 December 2023

Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B)Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B)

Structural highlights

4ap8 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.78Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MOC2B_HUMAN Molybdenum cofactor deficiency type B (MOCOD type B) [MIM:252150: Autosomal recessive disease which leads to the pleiotropic loss of all molybdoenzyme activities and is characterized by severe neurological damage, neonatal seizures and early childhood death. Note=The disease is caused by mutations affecting the gene represented in this entry.

Function

MOC2B_HUMAN Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.[1] [2]

References

  1. ↑ Leimkuhler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR. Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. J Biol Chem. 2003 Jul 11;278(28):26127-34. Epub 2003 May 5. PMID:12732628 doi:10.1074/jbc.M303092200
  2. ↑ Matthies A, Rajagopalan KV, Mendel RR, Leimkuhler S. Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5946-51. Epub 2004 Apr 8. PMID:15073332 doi:10.1073/pnas.0308191101

4ap8, resolution 2.78Å

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