2liu

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[[Image:2liu.png|left|200px]]
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==NMR structure of holo-ACPI domain from CurA module from Lyngbya majuscula==
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<StructureSection load='2liu' size='340' side='right' caption='[[2liu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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[[2liu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_majuscula Lyngbya majuscula]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LIU OCA]. <br>
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<b>Related:</b> [[2liw|2liw]]<br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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Polyketide synthases (PKS) and non-ribosomal peptide synthetases (NRPS) are large multidomain proteins present in microorganisms that produce bioactive compounds. Curacin A is such a bioactive compound with potent anti-proliferative activity. During its biosynthesis the growing substrate is bound covalently to an acyl carrier protein (ACP) that is able to access catalytic sites of neighboring domains for chain elongation and modification. While ACP domains usually occur as monomers, the curacin A cluster codes for a triplet ACP(ACP&lt;sub&gt;I&lt;/sub&gt;-ACP&lt;sub&gt;II&lt;/sub&gt;-ACP&lt;sub&gt;III&lt;/sub&gt;) within the CurA PKS module. We have determined the structure of the isolated holo ACP&lt;sub&gt;I&lt;/sub&gt; and show that the ACPs are independent of each other within this tridomain system. In addition, we have determined the structure of the 3-hydroxyl-3-methylglutaryl-loaded holo-ACP&lt;sub&gt;I&lt;/sub&gt;, which is the substrate for the unique halogenase (Hal) domain embedded within the CurA module. We have identified the interaction surface of both proteins using mutagenesis and MALDI-based identification of product formation. Amino acids affecting product formation are located on helices II and III of ACP&lt;sub&gt;I&lt;/sub&gt; and form a contiguous surface. Since the CurA Hal accepts substrate only when presented by one of the ACPs within the ACP&lt;sub&gt;I&lt;/sub&gt;-ACP&lt;sub&gt;II&lt;/sub&gt;-ACP&lt;sub&gt;III&lt;/sub&gt; tridomain, our data provide insight into the specificity of the chlorination reaction.
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Characterization of molecular interactions between ACP and halogenase domains in the curacin A polyketide synthase.,Busche AE, Gottstein D, Hein C, Ripin N, Pader I, Tufar P, Eisman EB, Gu L, Walsh CT, Loehr F, Sherman DH, Guntert P, Dotsch V ACS Chem Biol. 2011 Nov 21. PMID:22103656<ref>PMID:22103656</ref>
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The line below this paragraph, containing "STRUCTURE_2liu", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2liu| PDB=2liu | SCENE= }}
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===NMR structure of holo-ACPI domain from CurA module from Lyngbya majuscula===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_22103656}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 22103656 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22103656}}
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==About this Structure==
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[[2liu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_majuscula Lyngbya majuscula]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LIU OCA].
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==Reference==
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<ref group="xtra">PMID:022103656</ref><references group="xtra"/>
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[[Category: Lyngbya majuscula]]
[[Category: Lyngbya majuscula]]
[[Category: Busche, A E.]]
[[Category: Busche, A E.]]

Revision as of 08:40, 30 April 2014

NMR structure of holo-ACPI domain from CurA module from Lyngbya majuscula

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