1or5

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[[Image:1or5.gif|left|200px]]
 
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{{Structure
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==SOLUTION STRUCTURE OF THE HOLO-FORM OF THE FRENOLICIN ACYL CARRIER PROTEIN, MINIMIZED MEAN STRUCTURE==
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|PDB= 1or5 |SIZE=350|CAPTION= <scene name='initialview01'>1or5</scene>
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<StructureSection load='1or5' size='340' side='right'caption='[[1or5]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1or5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_roseofulvus Streptomyces roseofulvus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OR5 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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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=1or5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or5 OCA], [https://pdbe.org/1or5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1or5 RCSB], [https://www.ebi.ac.uk/pdbsum/1or5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1or5 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1or5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or5 OCA], [http://www.ebi.ac.uk/pdbsum/1or5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1or5 RCSB]</span>
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[https://www.uniprot.org/uniprot/Q54996_9ACTN Q54996_9ACTN]
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}}
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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/or/1or5_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=1or5 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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During polyketide biosynthesis, acyl carrier proteins (ACPs) perform the central role of transferring polyketide intermediates between active sites of polyketide synthase. The 4'-phosphopantetheine prosthetic group of a holo-ACP is a long and flexible arm that can reach into different active sites and provide a terminal sulfhydryl group for the attachment of acyl groups through a thioester linkage. We have determined the solution structure and characterized backbone dynamics of the holo form of the frenolicin acyl carrier protein (fren holo-ACP) by nuclear magnetic resonance (NMR). Unambiguous assignments were made for 433 hydrogen atoms, 333 carbon atoms, and 84 nitrogen atoms, representing a total of 94.6% of the assignable atoms in this protein. From 879 meaningful NOEs and 45 angle constraints, a family of 24 structures has been calculated. The solution structure is composed of three major alpha-helices packed in a bundle with three additional short helices in intervening loops; one of the short helices slowly exchanges between two conformations. Superposition of the major helical regions on the mean structure yields average atomic rmsd values of 0.49 +/- 0.09 and 0.91 +/- 0.08 A for backbone and non-hydrogen atoms, respectively. Although the three-helix bundle fold is conserved among acyl carrier proteins involved in fatty acid synthases and polyketide synthases, a detailed comparison revealed that ACPs from polyketide biosynthetic pathways are more related to each other in tertiary fold than to their homologues from fatty acid biosynthetic pathways. Comparison of the free form of ACPs (NMR structures of fren ACP and the Bacillus subtilis ACP) with the substrate-bound form of ACP (crystal structure of butyryl-ACP from Escherichia coli) suggests that conformational exchange plays a role in substrate binding.
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'''SOLUTION STRUCTURE OF THE HOLO-FORM OF THE FRENOLICIN ACYL CARRIER PROTEIN, MINIMIZED MEAN STRUCTURE'''
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Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein.,Li Q, Khosla C, Puglisi JD, Liu CW Biochemistry. 2003 Apr 29;42(16):4648-57. PMID:12705828<ref>PMID:12705828</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 1or5" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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During polyketide biosynthesis, acyl carrier proteins (ACPs) perform the central role of transferring polyketide intermediates between active sites of polyketide synthase. The 4'-phosphopantetheine prosthetic group of a holo-ACP is a long and flexible arm that can reach into different active sites and provide a terminal sulfhydryl group for the attachment of acyl groups through a thioester linkage. We have determined the solution structure and characterized backbone dynamics of the holo form of the frenolicin acyl carrier protein (fren holo-ACP) by nuclear magnetic resonance (NMR). Unambiguous assignments were made for 433 hydrogen atoms, 333 carbon atoms, and 84 nitrogen atoms, representing a total of 94.6% of the assignable atoms in this protein. From 879 meaningful NOEs and 45 angle constraints, a family of 24 structures has been calculated. The solution structure is composed of three major alpha-helices packed in a bundle with three additional short helices in intervening loops; one of the short helices slowly exchanges between two conformations. Superposition of the major helical regions on the mean structure yields average atomic rmsd values of 0.49 +/- 0.09 and 0.91 +/- 0.08 A for backbone and non-hydrogen atoms, respectively. Although the three-helix bundle fold is conserved among acyl carrier proteins involved in fatty acid synthases and polyketide synthases, a detailed comparison revealed that ACPs from polyketide biosynthetic pathways are more related to each other in tertiary fold than to their homologues from fatty acid biosynthetic pathways. Comparison of the free form of ACPs (NMR structures of fren ACP and the Bacillus subtilis ACP) with the substrate-bound form of ACP (crystal structure of butyryl-ACP from Escherichia coli) suggests that conformational exchange plays a role in substrate binding.
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*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1OR5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_roseofulvus Streptomyces roseofulvus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OR5 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein., Li Q, Khosla C, Puglisi JD, Liu CW, Biochemistry. 2003 Apr 29;42(16):4648-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12705828 12705828]
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[[Category: Single protein]]
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[[Category: Streptomyces roseofulvus]]
[[Category: Streptomyces roseofulvus]]
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[[Category: Khosla, C.]]
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[[Category: Khosla C]]
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[[Category: Li, Q.]]
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[[Category: Li Q]]
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[[Category: Liu, C W.]]
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[[Category: Liu CW]]
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[[Category: Puglisi, J.]]
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[[Category: Puglisi J]]
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[[Category: acp]]
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[[Category: acyl carrier protein]]
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[[Category: biosynthesis]]
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[[Category: frenolicin]]
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[[Category: holo]]
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[[Category: pk]]
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[[Category: polyketide synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:49:14 2008''
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Current revision

SOLUTION STRUCTURE OF THE HOLO-FORM OF THE FRENOLICIN ACYL CARRIER PROTEIN, MINIMIZED MEAN STRUCTURE

PDB ID 1or5

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