2liu
From Proteopedia
(Difference between revisions)
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<StructureSection load='2liu' size='340' side='right' caption='[[2liu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2liu' size='340' side='right' caption='[[2liu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[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> | + | <table><tr><td colspan='2'>[[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> |
| - | <b>[[Related_structure|Related:]]</b> [[2liw|2liw]]< | + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2liw|2liw]]</td></tr> |
| - | <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>< | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">curA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158786 Lyngbya majuscula])</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2liu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2liu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2liu RCSB], [http://www.ebi.ac.uk/pdbsum/2liu PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> |
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2liu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2liu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2liu RCSB], [http://www.ebi.ac.uk/pdbsum/2liu PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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<sub>I</sub>-ACP<sub>II</sub>-ACP<sub>III</sub>) within the CurA PKS module. We have determined the structure of the isolated holo ACP<sub>I</sub> 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<sub>I</sub>, 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<sub>I</sub> and form a contiguous surface. Since the CurA Hal accepts substrate only when presented by one of the ACPs within the ACP<sub>I</sub>-ACP<sub>II</sub>-ACP<sub>III</sub> tridomain, our data provide insight into the specificity of the chlorination reaction. | 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<sub>I</sub>-ACP<sub>II</sub>-ACP<sub>III</sub>) within the CurA PKS module. We have determined the structure of the isolated holo ACP<sub>I</sub> 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<sub>I</sub>, 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<sub>I</sub> and form a contiguous surface. Since the CurA Hal accepts substrate only when presented by one of the ACPs within the ACP<sub>I</sub>-ACP<sub>II</sub>-ACP<sub>III</sub> tridomain, our data provide insight into the specificity of the chlorination reaction. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:57, 1 May 2014
NMR structure of holo-ACPI domain from CurA module from Lyngbya majuscula
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Categories: Lyngbya majuscula | Busche, A E. | Dotsch, V. | Eisman, E B. | Gottstein, D. | Gu, L. | Guntert, P. | Hein, C. | Loehr, F. | Pader, I. | Ripin, N. | Sherman, D H. | Tufar, P. | Walsh, C T. | Holo state | Transferase
