1hy8

From Proteopedia

(Difference between revisions)

Current revision

SOLUTION STRUCTURE OF B. SUBTILIS ACYL CARRIER PROTEIN

Structural highlights

1hy8 is a 1 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACP_BACSU Carrier of the growing fatty acid chain in fatty acid biosynthesis.

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

BACKGROUND: Acyl carrier protein (ACP) is a fundamental component of fatty acid biosynthesis in which the fatty acid chain is elongated by the fatty acid synthetase system while attached to the 4'-phosphopantetheine prosthetic group (4'-PP) of ACP. Activation of ACP is mediated by holo-acyl carrier protein synthase (ACPS) when ACPS transfers the 4'-PP moiety from coenzyme A (CoA) to Ser36 of apo-ACP. Both ACP and ACPS have been identified as essential for E. coli viability and potential targets for development of antibiotics. RESULTS: The solution structure of B. subtilis ACP (9 kDa) has been determined using two-dimensional and three-dimensional heteronuclear NMR spectroscopy. A total of 22 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 1,050 experimental NMR restraints. The atomic rmsd about the mean coordinate positions for the 22 structures is 0.45 +/- 0.08 A for the backbone atoms and 0.93 +/- 0.07 A for all atoms. The overall ACP structure consists of a four alpha-helical bundle in which 4'-PP is attached to the conserved Ser36 that is located in alpha helix II. CONCLUSIONS: Structural data were collected for both the apo and holo forms of ACP that suggest that the two forms of ACP are essentially identical. Comparison of the published structures for E. coli ACP and actinorhodin polyketide synthase acyl carrier protein (act apo-ACP) from Streptomyces coelicolor A3(2) with B. subtilis ACP indicates similar secondary structure elements but an extremely large rmsd between the three ACP structures (>4.3 A). The structural difference between B. subtilis ACP and both E. coli and act apo-ACP is not attributed to an inherent difference in the proteins, but is probably a result of a limitation in the methodology available for the analysis for E. coli and act apo-ACP. Comparison of the structure of free ACP with the bound form of ACP in the ACP-ACPS complex reveals a displacement of helix II in the vicinity of Ser36. The induced perturbation of ACP by ACPS positions Ser36 proximal to coenzyme A and aligns the dipole of helix II to initiate transfer of 4'-PP to ACP.

Solution structure of B. subtilis acyl carrier protein.,Xu GY, Tam A, Lin L, Hixon J, Fritz CC, Powers R Structure. 2001 Apr 4;9(4):277-87. PMID:11525165^[1]

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

References

↑ Xu GY, Tam A, Lin L, Hixon J, Fritz CC, Powers R. Solution structure of B. subtilis acyl carrier protein. Structure. 2001 Apr 4;9(4):277-87. PMID:11525165

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/1hy8"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE OF B. SUBTILIS ACYL CARRIER PROTEIN==
-<StructureSection load='1hy8' size='340' side='right' caption='[[1hy8]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1hy8' size='340' side='right'caption='[[1hy8]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hy8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HY8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hy8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HY8 FirstGlance]. <br>
-</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=1hy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hy8 OCA], [http://pdbe.org/1hy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hy8 RCSB], [http://www.ebi.ac.uk/pdbsum/1hy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hy8 ProSAT]</span></td></tr>
+</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=1hy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hy8 OCA], [https://pdbe.org/1hy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hy8 RCSB], [https://www.ebi.ac.uk/pdbsum/1hy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hy8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACP_BACSU ACP_BACSU]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.
+[https://www.uniprot.org/uniprot/ACP_BACSU ACP_BACSU] Carrier of the growing fatty acid chain in fatty acid biosynthesis.
 == 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/hy/1hy8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/1hy8_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 ==See Also==
-*[[Acyl carrier protein|Acyl carrier protein]]
+*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Fritz, C C]]
+[[Category: Bacillus subtilis]]
-[[Category: Hixon, J]]
+[[Category: Large Structures]]
-[[Category: Lin, L]]
+[[Category: Fritz CC]]
-[[Category: Power, R]]
+[[Category: Hixon J]]
-[[Category: Tam, A]]
+[[Category: Lin L]]
-[[Category: Xu, G Y]]
+[[Category: Power R]]
-[[Category: 4' phosphopantetheine prosthetic group]]
+[[Category: Tam A]]
-[[Category: Acp]]
+[[Category: Xu G-Y]]
-[[Category: Apo-acp]]
-[[Category: Fatty acid biosynthesis]]
-[[Category: Holo-acp]]
-[[Category: Lipid binding protein]]

1hy8

From Proteopedia

Current revision

SOLUTION STRUCTURE OF B. SUBTILIS ACYL CARRIER PROTEIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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