1los: Difference between revisions

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[[Image:1los.gif|left|200px]]


{{Structure
==crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP==
|PDB= 1los |SIZE=350|CAPTION= <scene name='initialview01'>1los</scene>, resolution 1.90&Aring;
<StructureSection load='1los' size='340' side='right'caption='[[1los]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=UP6:6-AZA URIDINE 5&#39;-MONOPHOSPHATE'>UP6</scene>
<table><tr><td colspan='2'>[[1los]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LOS FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UP6:6-AZA+URIDINE+5-MONOPHOSPHATE'>UP6</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=1los FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1los OCA], [https://pdbe.org/1los PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1los RCSB], [https://www.ebi.ac.uk/pdbsum/1los PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1los ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYRF_METTH PYRF_METTH] Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).[HAMAP-Rule:MF_01200_A]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lo/1los_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1los ConSurf].
<div style="clear:both"></div>


'''crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP'''
==See Also==
 
*[[Uridine 5'-monophosphate synthase 3D structures|Uridine 5'-monophosphate synthase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structures of the enzyme orotidine-5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with its product UMP and the inhibitors 6-hydroxyuridine 5'-phosphate (BMP), XMP, and CMP are reported. A mutant version of the protein, in which four residues of the flexible phosphate-binding loop (180)Gly-Gly(190) were removed and Arg(203) was replaced by alanine, was also analyzed. The XMP and CMP complexes reveal a ligand-binding mode that is distinct from the one identified previously with the aromatic rings located outside the binding pocket. A potential pathway for ligand binding is discussed.
[[Category: Large Structures]]
 
[[Category: Methanothermobacter thermautotrophicus str. Delta H]]
==About this Structure==
[[Category: Pai EF]]
1LOS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOS OCA].
[[Category: Wu N]]
 
==Reference==
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase., Wu N, Pai EF, J Biol Chem. 2002 Aug 2;277(31):28080-7. Epub 2002 May 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12011084 12011084]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Orotidine-5'-phosphate decarboxylase]]
[[Category: Single protein]]
[[Category: Pai, E F.]]
[[Category: Wu, N.]]
[[Category: UP6]]
[[Category: tim barrel]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:39:14 2008''

Latest revision as of 10:34, 14 February 2024

crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMPcrystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP

Structural highlights

1los is a 4 chain structure with sequence from Methanothermobacter thermautotrophicus str. Delta H. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYRF_METTH Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).[HAMAP-Rule:MF_01200_A]

Evolutionary Conservation

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

See Also

1los, resolution 1.90Å

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