1fma: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1fma' size='340' side='right'caption='[[1fma]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='1fma' size='340' side='right'caption='[[1fma]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fma]] is a 2 chain structure with sequence from [https://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=1FMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fma]] 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=1FMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.58&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fmo|1fmo]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=1fma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fma OCA], [https://pdbe.org/1fma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fma RCSB], [https://www.ebi.ac.uk/pdbsum/1fma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fma 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=1fma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fma OCA], [https://pdbe.org/1fma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fma RCSB], [https://www.ebi.ac.uk/pdbsum/1fma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fma ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MOAD_ECOLI MOAD_ECOLI]] Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.<ref>PMID:17223713</ref> [[https://www.uniprot.org/uniprot/MOAE_ECOLI MOAE_ECOLI]] Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD.
[https://www.uniprot.org/uniprot/MOAD_ECOLI MOAD_ECOLI] Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.<ref>PMID:17223713</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 20: Line 20:
</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/main_output.php?pdb_ID=1fma ConSurf].
</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/main_output.php?pdb_ID=1fma ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes, including humans. Genetic deficiencies of enzymes involved in Moco biosynthesis in humans lead to a severe and usually fatal disease. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of MPT is generated by MPT synthase, which consists of a large and small subunits. The 1.45 A resolution crystal structure of MPT synthase reveals a heterotetrameric protein in which the C-terminus of each small subunit is inserted into a large subunit to form the active site. In the activated form of the enzyme this C-terminus is present as a thiocarboxylate. In the structure of a covalent complex of MPT synthase, an isopeptide bond is present between the C-terminus of the small subunit and a Lys side chain in the large subunit. The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway.
Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation.,Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H Nat Struct Biol. 2001 Jan;8(1):42-6. PMID:11135669<ref>PMID:11135669</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fma" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rajagolpalan, K V]]
[[Category: Rajagolpalan KV]]
[[Category: Rudolph, M J]]
[[Category: Rudolph MJ]]
[[Category: Schindelin, H]]
[[Category: Schindelin H]]
[[Category: Wuebbens, M M]]
[[Category: Wuebbens MM]]
[[Category: Isopeptide bond]]
[[Category: Molybdenum cofactor biosynthesis]]
[[Category: Transferase]]

Latest revision as of 10:16, 7 February 2024

MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)

Structural highlights

1fma is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.58Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MOAD_ECOLI Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Schmitz J, Wuebbens MM, Rajagopalan KV, Leimkuhler S. Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Biochemistry. 2007 Jan 23;46(3):909-16. PMID:17223713 doi:http://dx.doi.org/10.1021/bi062011w

1fma, resolution 1.58Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1fma&oldid=4043606"