2bmb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
<StructureSection load='2bmb' size='340' side='right' caption='[[2bmb]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2bmb' size='340' side='right' caption='[[2bmb]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bmb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2bmb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BMB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMM:PTERIN-6-YL-METHYL-MONOPHOSPHATE'>PMM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMM:PTERIN-6-YL-METHYL-MONOPHOSPHATE'>PMM</scene></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=2bmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bmb RCSB], [http://www.ebi.ac.uk/pdbsum/2bmb 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=2bmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmb OCA], [http://pdbe.org/2bmb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bmb RCSB], [http://www.ebi.ac.uk/pdbsum/2bmb PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 24: | Line 24: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2bmb" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 31: | Line 32: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 18824]] | ||
[[Category: Berglez, J]] | [[Category: Berglez, J]] | ||
[[Category: Fernley, R T]] | [[Category: Fernley, R T]] | ||
Revision as of 19:20, 11 September 2015
X-RAY STRUCTURE OF THE BIFUNCTIONAL 6-HYDROXYMETHYL-7,8-DIHYDROXYPTERIN PYROPHOSPHOKINASE DIHYDROPTEROATE SYNTHASE FROM SACCHAROMYCES CEREVISIAEX-RAY STRUCTURE OF THE BIFUNCTIONAL 6-HYDROXYMETHYL-7,8-DIHYDROXYPTERIN PYROPHOSPHOKINASE DIHYDROPTEROATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn Saccharomyces cerevisiae and other fungi, the enzymes dihydroneopterin aldolase, 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and dihydropteroate synthase (DHPS) are encoded by a polycistronic gene that is translated into a single polypeptide having all three functions. These enzymatic functions are essential to both prokaryotes and lower eukaryotes, and catalyse sequential reactions in folate biosynthesis. Deletion or disruption of either function leads to cell death. These enzymes are absent from mammals and thus make ideal antimicrobial targets. DHPS is currently the target of antifolate therapy for a number of infectious diseases, and its activity is inhibited by sulfonamides and sulfones. These drugs are typically used as part of a synergistic cocktail with the 2,4-diaminopyrimidines that inhibit dihydrofolate reductase. A gene encoding the S.cerevisiae HPPK and DHPS enzymes has been cloned and expressed in Escherichia coli. A complex of the purified bifunctional polypeptide with a pterin monophosphate substrate analogue has been crystallized, and its structure solved by molecular replacement and refined to 2.3A resolution. The polypeptide consists of two structural domains, each of which closely resembles its respective monofunctional bacterial HPPK and DHPS counterpart. The mode of ligand binding is similar to that observed in the bacterial enzymes. The association between the domains within the polypeptide as well as the quaternary association of the polypeptide via its constituent DHPS domains provide insight into the assembly of the trifunctional enzyme in S.cerevisiae and probably other fungal species. The three-dimensional structure of the bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase of Saccharomyces cerevisiae.,Lawrence MC, Iliades P, Fernley RT, Berglez J, Pilling PA, Macreadie IG J Mol Biol. 2005 May 6;348(3):655-70. PMID:15826662[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||