5ov4: Difference between revisions
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==Bacillus megaterium porphobilinogen deaminase D82A mutant== | ==Bacillus megaterium porphobilinogen deaminase D82A mutant== | ||
<StructureSection load='5ov4' size='340' side='right' caption='[[5ov4]], [[Resolution|resolution]] 2.69Å' scene=''> | <StructureSection load='5ov4' size='340' side='right'caption='[[5ov4]], [[Resolution|resolution]] 2.69Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ov4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ov4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OV4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.692Å</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=5ov4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ov4 OCA], [https://pdbe.org/5ov4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ov4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ov4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ov4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/Q8GCA8_PRIMG Q8GCA8_PRIMG] Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.[ARBA:ARBA00002869][HAMAP-Rule:MF_00260] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 5ov4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ov4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Porphobilinogen Deaminase|Porphobilinogen Deaminase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Priestia megaterium]] | ||
[[Category: Coker | [[Category: Coker AR]] | ||
[[Category: Cooper | [[Category: Cooper JB]] | ||
[[Category: Erskine | [[Category: Erskine P]] | ||
[[Category: Guo | [[Category: Guo J]] | ||
[[Category: Wood | [[Category: Wood SP]] | ||
Latest revision as of 04:25, 28 December 2023
Bacillus megaterium porphobilinogen deaminase D82A mutantBacillus megaterium porphobilinogen deaminase D82A mutant
Structural highlights
FunctionQ8GCA8_PRIMG Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.[ARBA:ARBA00002869][HAMAP-Rule:MF_00260] Publication Abstract from PubMedThe enzyme porphobilinogen deaminase (PBGD) is one of the key enzymes in tetrapyrrole biosynthesis. It catalyses the formation of a linear tetrapyrrole from four molecules of the substrate porphobilinogen (PBG). It has a dipyrromethane cofactor (DPM) in the active site which is covalently linked to a conserved cysteine residue through a thioether bridge. The substrate molecules are linked to the cofactor in a stepwise head-to-tail manner during the reaction, which is catalysed by a conserved aspartate residue: Asp82 in the B. megaterium enzyme. Three mutations have been made affecting Asp82 (D82A, D82E and D82N) and their crystal structures have been determined at resolutions of 2.7, 1.8 and 1.9 A, respectively. These structures reveal that whilst the D82E mutant possesses the DPM cofactor, in the D82N and D82A mutants the cofactor is likely to be missing, incompletely assembled or disordered. Comparison of the mutant PBGD structures with that of the wild-type enzyme shows that there are significant domain movements and suggests that the enzyme adopts `open' and `closed' conformations, potentially in response to substrate binding. Structural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.,Guo J, Erskine P, Coker AR, Wood SP, Cooper JB Acta Crystallogr F Struct Biol Commun. 2017 Nov 1;73(Pt 11):612-620. doi:, 10.1107/S2053230X17015436. Epub 2017 Oct 30. PMID:29095155[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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