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New page: left|200px<br /><applet load="1klp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1klp" /> '''The Solution Structure of Acyl Carrier Prote...
 
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[[Image:1klp.jpg|left|200px]]<br /><applet load="1klp" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1klp" />
'''The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis'''<br />


==Overview==
==The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis==
Acyl carrier protein (ACP) performs the essential function of shuttling, the intermediates between the enzymes that constitute the type II fatty, acid synthase system. Mycobacterium tuberculosis is unique in producing, extremely long mycolic acids, and tubercular ACP, AcpM, is also unique in, possessing a longer carboxyl terminus than other ACPs. We determined the, solution structure of AcpM using protein NMR spectroscopy to define the, similarities and differences between AcpM and the typical structures. The, amino-terminal region of the structure is well defined and consists of, four helices arranged in a right-handed bundle held together by, interhelical hydrophobic interactions similar to the structures of other, bacterial ACPs. The unique carboxyl-terminal extension from helix IV has a, "melted down" feature, and the end of the molecule is a random coil. A, comparison of the apo- and holo-forms of AcpM revealed that the, 4'-phosphopantetheine group oscillates between two states; in one it is, bound to a hydrophobic groove on the surface of AcpM, and in another it is, solvent-exposed. The similarity between AcpM and other ACPs reveals the, conserved structural motif that is recognized by all type II enzymes., However, the function of the coil domain extending from helix IV to the, carboxyl terminus remains enigmatic, but its structural characteristics, suggest that it may interact with the very long chain intermediates in, mycolic acid biosynthesis or control specific protein-protein, interactions.
<StructureSection load='1klp' size='340' side='right'caption='[[1klp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1klp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KLP FirstGlance]. <br>
</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=1klp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1klp OCA], [https://pdbe.org/1klp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1klp RCSB], [https://www.ebi.ac.uk/pdbsum/1klp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1klp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACPM_MYCTU ACPM_MYCTU] Acyl carrier protein involved in meromycolate extension (By similarity).
== 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/kl/1klp_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=1klp ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1KLP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KLP OCA].
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
 
*[[Proteins from Mycobacterium tuberculosis|Proteins from Mycobacterium tuberculosis]]
==Reference==
__TOC__
The solution structure of acyl carrier protein from Mycobacterium tuberculosis., Wong HC, Liu G, Zhang YM, Rock CO, Zheng J, J Biol Chem. 2002 May 3;277(18):15874-80. Epub 2002 Feb 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11825906 11825906]
</StructureSection>
[[Category: Mycobacterium tuberculosis]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Liu, G.]]
[[Category: Liu G]]
[[Category: Rock, C.O.]]
[[Category: Rock CO]]
[[Category: Wong, H.C.]]
[[Category: Wong HC]]
[[Category: Zhang, Y.M.]]
[[Category: Zhang Y-M]]
[[Category: Zheng, J.]]
[[Category: Zheng J]]
[[Category: four-helix bundle]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:20:50 2007''

Latest revision as of 08:01, 3 April 2024

The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis

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