2bmb

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{{Seed}}
 
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[[Image:2bmb.png|left|200px]]
 
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==X-ray structure of the bifunctional 6-hydroxymethyl-7,8- dihydroxypterin pyrophosphokinase dihydropteroate synthase from Saccharomyces cerevisiae==
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The line below this paragraph, containing "STRUCTURE_2bmb", creates the "Structure Box" on the page.
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<StructureSection load='2bmb' size='340' side='right'caption='[[2bmb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bmb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2BMB FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMM:PTERIN-6-YL-METHYL-MONOPHOSPHATE'>PMM</scene></td></tr>
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{{STRUCTURE_2bmb| PDB=2bmb | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmb OCA], [https://pdbe.org/2bmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bmb RCSB], [https://www.ebi.ac.uk/pdbsum/2bmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bmb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FOL1_YEAST FOL1_YEAST] Catalyzes three sequential steps of tetrahydrofolate biosynthesis.<ref>PMID:15169867</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/2bmb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bmb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In 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.
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===X-RAY STRUCTURE OF THE BIFUNCTIONAL 6-HYDROXYMETHYL-7,8-DIHYDROXYPTERIN PYROPHOSPHOKINASE DIHYDROPTEROATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE===
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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<ref>PMID:15826662</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2bmb" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15826662}}, adds the Publication Abstract to the page
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*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15826662 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15826662}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2BMB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMB OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15826662 15826662]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Berglez J]]
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[[Category: Berglez, J.]]
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[[Category: Fernley RT]]
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[[Category: Fernley, R T.]]
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[[Category: Iliades P]]
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[[Category: Iliades, P.]]
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[[Category: Lawrence MC]]
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[[Category: Lawrence, M C.]]
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[[Category: Macreadie IG]]
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[[Category: Macreadie, I G.]]
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[[Category: Pilling PA]]
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[[Category: Pilling, P A.]]
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[[Category: Folate biosynthesis]]
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[[Category: Ligase]]
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[[Category: Multifunctional enzyme]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:52:25 2008''
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Current revision

X-ray structure of the bifunctional 6-hydroxymethyl-7,8- dihydroxypterin pyrophosphokinase dihydropteroate synthase from Saccharomyces cerevisiae

PDB ID 2bmb

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