1mzj

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the Priming beta-Ketosynthase from the R1128 Polyketide Biosynthetic Pathway

Structural highlights

1mzj is a 2 chain structure with sequence from Streptomyces sp. R1128. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABH_STRLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate preference for butyryl-CoA and can tolerate branched substrates. Can also prime acyl-CoA. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Involved in the biosynthesis of R1128 polyketide.^[1]

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 PubMed

ZhuH is a priming ketosynthase that initiates the elongation of the polyketide chain in the biosynthetic pathway of a type II polyketide, R1128. The crystal structure of ZhuH in complex with the priming substrate acetyl-CoA reveals an extensive loop region at the dimer interface that appears to affect the selectivity for the primer unit. Acetyl-CoA is bound in a 20 A-long channel, which placed the acetyl group against the catalytic triad. Analysis of the primer unit binding site in ZhuH suggests that it can accommodate acyl chains that are two to four carbons long. Selectivity and primer unit size appear to involve the side chains of three residues on the loops close to the dimer interface that constitute the bottom of the substrate binding pocket.

Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway.,Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM Structure. 2002 Nov;10(11):1559-68. PMID:12429097^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Meadows ES, Khosla C. In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase. Biochemistry. 2001 Dec 11;40(49):14855-61. PMID:11732905
↑ Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM. Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway. Structure. 2002 Nov;10(11):1559-68. PMID:12429097

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mzj"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mzj' size='340' side='right'caption='[[1mzj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mzj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp._r1128 Streptomyces sp. r1128]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MZJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mzj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._R1128 Streptomyces sp. R1128]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</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]] 2.1&#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;'>[[1ebl|1ebl]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">zhuH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=140437 Streptomyces sp. R1128])</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=1mzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzj OCA], [https://pdbe.org/1mzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mzj RCSB], [https://www.ebi.ac.uk/pdbsum/1mzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzj ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1mzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzj OCA], [http://pdbe.org/1mzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mzj RCSB], [http://www.ebi.ac.uk/pdbsum/1mzj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FABH_STRLI FABH_STRLI]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate preference for butyryl-CoA and can tolerate branched substrates. Can also prime acyl-CoA. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Involved in the biosynthesis of R1128 polyketide.<ref>PMID:11732905</ref>
+[https://www.uniprot.org/uniprot/FABH_STRLI FABH_STRLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate preference for butyryl-CoA and can tolerate branched substrates. Can also prime acyl-CoA. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Involved in the biosynthesis of R1128 polyketide.<ref>PMID:11732905</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mzj_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 39: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Streptomyces sp. r1128]]
+[[Category: Streptomyces sp. R1128]]
-[[Category: Connell, J O]]
+[[Category: Keatinge-Clay A]]
-[[Category: Keatinge-Clay, A]]
+[[Category: Khosla C]]
-[[Category: Khosla, C]]
+[[Category: Meadows ES]]
-[[Category: Meadows, E S]]
+[[Category: Miercke LJW]]
-[[Category: Miercke, L J.W]]
+[[Category: O'Connell J]]
-[[Category: Pan, H]]
+[[Category: Pan H]]
-[[Category: Stroud, R M]]
+[[Category: Stroud RM]]
-[[Category: Tsai, S C]]
+[[Category: Tsai SC]]
-[[Category: Aromatic polyketide]]
-[[Category: Beta-ketosynthase]]
-[[Category: Biosynthetic engineering]]
-[[Category: Catalytic triad]]
-[[Category: Transferase]]

1mzj

From Proteopedia

Current revision

Crystal Structure of the Priming beta-Ketosynthase from the R1128 Polyketide Biosynthetic Pathway

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox