2ju2: Difference between revisions

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-{{Seed}}
-[[Image:2ju2.png|left|200px]]
-<!--
+==Minimized mean solution structure of the acyl carrier protein domain from module 2 of 6-deoxyerythronolide B synthase (DEBS)==
-The line below this paragraph, containing "STRUCTURE_2ju2", creates the "Structure Box" on the page.
+<StructureSection load='2ju2' size='340' side='right'caption='[[2ju2]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ju2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JU2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ju2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ju2 OCA], [https://pdbe.org/2ju2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ju2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ju2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ju2 ProSAT]</span></td></tr>
-{{STRUCTURE_2ju2|  PDB=2ju2  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ERYA1_SACER ERYA1_SACER]
+== 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/ju/2ju2_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=2ju2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Polyketides are a medicinally important class of natural products. The architecture of modular polyketide synthases (PKSs), composed of multiple covalently linked domains grouped into modules, provides an attractive framework for engineering novel polyketide-producing assemblies. However, impaired domain-domain interactions can compromise the efficiency of engineered polyketide biosynthesis. To facilitate the study of these domain-domain interactions, we have used nuclear magnetic resonance (NMR) spectroscopy to determine the first solution structure of an acyl carrier protein (ACP) domain from a modular PKS, 6-deoxyerythronolide B synthase (DEBS). The tertiary fold of this 10-kD domain is a three-helical bundle; an additional short helix in the second loop also contributes to the core helical packing. Superposition of residues 14-94 of the ensemble on the mean structure yields an average atomic RMSD of 0.64 +/- 0.09 Angstrom for the backbone atoms (1.21 +/- 0.13 Angstrom for all non-hydrogen atoms). The three major helices superimpose with a backbone RMSD of 0.48 +/- 0.10 Angstrom (0.99 +/- 0.11 Angstrom for non-hydrogen atoms). Based on this solution structure, homology models were constructed for five other DEBS ACP domains. Comparison of their steric and electrostatic surfaces at the putative interaction interface (centered on helix II) suggests a model for protein-protein recognition of ACP domains, consistent with the previously observed specificity. Site-directed mutagenesis experiments indicate that two of the identified residues influence the specificity of ACP recognition.
-===Minimized mean solution structure of the acyl carrier protein domain from module 2 of 6-deoxyerythronolide B synthase (DEBS)===
+Solution structure and proposed domain domain recognition interface of an acyl carrier protein domain from a modular polyketide synthase.,Alekseyev VY, Liu CW, Cane DE, Puglisi JD, Khosla C Protein Sci. 2007 Oct;16(10):2093-107. PMID:17893358<ref>PMID:17893358</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ju2" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17893358}}, adds the Publication Abstract to the page
+*[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17893358 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17893358}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-JU2 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JU2 OCA].
-==Reference==
-<ref group="xtra">PMID:17893358</ref><references group="xtra"/>
-[[Category: Erythronolide synthase]]
 [[Category: Saccharopolyspora erythraea]]
-[[Category: Alekseyev, V Y.]]
+[[Category: Alekseyev VY]]
-[[Category: Khosla, C.]]
+[[Category: Khosla C]]
-[[Category: Liu, C W.]]
+[[Category: Liu CW]]
-[[Category: Puglisi, J D.]]
+[[Category: Puglisi JD]]
-[[Category: Acyltransferase]]
-[[Category: Alpha-helical bundle]]
-[[Category: Antibiotic biosynthesis]]
-[[Category: Carrier protein domain]]
-[[Category: Modular polyketide synthase]]
-[[Category: Multifunctional enzyme]]
-[[Category: Nadp]]
-[[Category: Phosphopantetheine]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:10:11 2009''