2afd

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(New page: 200px<br /><applet load="2afd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2afd" /> '''Solution Structure of Asl1650, an Acyl Carri...)
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==Overview==
==Overview==
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Cyanobacteria, such as Anabaena, produce a variety of bioactive natural, products via polyketide synthases (PKS), nonribosomal peptide synthetases, (NRPS), and hybrid peptide/polyketide pathways. The protein Asl1650, which, is a member of the acyl carrier protein family from the cyanobacterium, Anabaena sp. PCC 7120, is encoded in a region of the Anabaena genome that, is rich in PKS and NRPS genes. To gain new insight into the physiological, role of acyl carriers in Anabaena, the solution structure of Asl1650 has, been solved by NMR spectroscopy. The protein adopts a twisted antiparallel, four-helix bundle fold, with a variant phosphopantetheine-attachment motif, positioned at the start of the second helix. Structure comparisons with, proteins from other organisms suggest a likely physiological function as a, discrete peptidyl carrier protein.
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Cyanobacteria, such as Anabaena, produce a variety of bioactive natural products via polyketide synthases (PKS), nonribosomal peptide synthetases (NRPS), and hybrid peptide/polyketide pathways. The protein Asl1650, which is a member of the acyl carrier protein family from the cyanobacterium Anabaena sp. PCC 7120, is encoded in a region of the Anabaena genome that is rich in PKS and NRPS genes. To gain new insight into the physiological role of acyl carriers in Anabaena, the solution structure of Asl1650 has been solved by NMR spectroscopy. The protein adopts a twisted antiparallel four-helix bundle fold, with a variant phosphopantetheine-attachment motif positioned at the start of the second helix. Structure comparisons with proteins from other organisms suggest a likely physiological function as a discrete peptidyl carrier protein.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Herrmann, T.]]
[[Category: Herrmann, T.]]
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[[Category: JCSG, Joint.Center.for.Structural.Genomics.]]
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[[Category: JCSG, Joint Center for Structural Genomics.]]
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[[Category: Johnson, M.A.]]
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[[Category: Johnson, M A.]]
[[Category: Peti, W.]]
[[Category: Peti, W.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: Wuthrich, K.]]
[[Category: Wuthrich, K.]]
[[Category: jcsg]]
[[Category: jcsg]]
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[[Category: twisted antiparallel helical bundle; acyl carrier protein family]]
[[Category: twisted antiparallel helical bundle; acyl carrier protein family]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:01:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:26:59 2008''

Revision as of 14:27, 21 February 2008


2afd

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Solution Structure of Asl1650, an Acyl Carrier Protein from Anabaena sp. PCC 7120 with a Variant Phosphopantetheinylation-Site Sequence

Overview

Cyanobacteria, such as Anabaena, produce a variety of bioactive natural products via polyketide synthases (PKS), nonribosomal peptide synthetases (NRPS), and hybrid peptide/polyketide pathways. The protein Asl1650, which is a member of the acyl carrier protein family from the cyanobacterium Anabaena sp. PCC 7120, is encoded in a region of the Anabaena genome that is rich in PKS and NRPS genes. To gain new insight into the physiological role of acyl carriers in Anabaena, the solution structure of Asl1650 has been solved by NMR spectroscopy. The protein adopts a twisted antiparallel four-helix bundle fold, with a variant phosphopantetheine-attachment motif positioned at the start of the second helix. Structure comparisons with proteins from other organisms suggest a likely physiological function as a discrete peptidyl carrier protein.

About this Structure

2AFD is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.

Reference

Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence., Johnson MA, Peti W, Herrmann T, Wilson IA, Wuthrich K, Protein Sci. 2006 May;15(5):1030-41. Epub 2006 Apr 5. PMID:16597827

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