1rtt

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(New page: 200px<br /><applet load="1rtt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rtt, resolution 1.28&Aring;" /> '''Crystal structure de...)
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[[Image:1rtt.gif|left|200px]]<br /><applet load="1rtt" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rtt.gif|left|200px]]<br /><applet load="1rtt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rtt, resolution 1.28&Aring;" />
caption="1rtt, resolution 1.28&Aring;" />
'''Crystal structure determination of a putative NADH-dependent reductase using sulfur anomalous signal'''<br />
'''Crystal structure determination of a putative NADH-dependent reductase using sulfur anomalous signal'''<br />
==Overview==
==Overview==
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The availability of high-intensity synchrotron facilities, technological, advances in data-collection techniques and improved data-reduction and, crystallographic software have ushered in a new era in high-throughput, macromolecular crystallography. Here, the de novo automated crystal, structure determination at 1.28 A resolution of an NAD(P)H-dependent FMN, reductase flavoprotein from Pseudomonas aeruginosa PA01-derived protein, Q9I4D4 using the anomalous signal from an unusually small number of S, atoms is reported. Although this protein lacks the flavodoxin key, fingerprint motif [(T/S)XTGXT], it has been confirmed to bind flavin, mononucleotide and the binding site was identified via X-ray, crystallography. This protein contains a novel flavin, mononucleotide-binding site GSLRSGSYN, which has not been previously, reported. Detailed statistics pertaining to sulfur phasing and other, factors contributing to structure determination are discussed. Structural, comparisons of the apoenzyme and the protein complexed with flavin, mononucleotide show conformational changes on cofactor binding., NADPH-dependent activity has been confirmed with biochemical assays.
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The availability of high-intensity synchrotron facilities, technological advances in data-collection techniques and improved data-reduction and crystallographic software have ushered in a new era in high-throughput macromolecular crystallography. Here, the de novo automated crystal structure determination at 1.28 A resolution of an NAD(P)H-dependent FMN reductase flavoprotein from Pseudomonas aeruginosa PA01-derived protein Q9I4D4 using the anomalous signal from an unusually small number of S atoms is reported. Although this protein lacks the flavodoxin key fingerprint motif [(T/S)XTGXT], it has been confirmed to bind flavin mononucleotide and the binding site was identified via X-ray crystallography. This protein contains a novel flavin mononucleotide-binding site GSLRSGSYN, which has not been previously reported. Detailed statistics pertaining to sulfur phasing and other factors contributing to structure determination are discussed. Structural comparisons of the apoenzyme and the protein complexed with flavin mononucleotide show conformational changes on cofactor binding. NADPH-dependent activity has been confirmed with biochemical assays.
==About this Structure==
==About this Structure==
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1RTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RTT OCA].
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1RTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTT OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Agarwal, R.]]
[[Category: Agarwal, R.]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Swaminathan, S.]]
[[Category: Swaminathan, S.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:14:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:29 2008''

Revision as of 12:54, 21 February 2008


1rtt, resolution 1.28Å

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Crystal structure determination of a putative NADH-dependent reductase using sulfur anomalous signal

Overview

The availability of high-intensity synchrotron facilities, technological advances in data-collection techniques and improved data-reduction and crystallographic software have ushered in a new era in high-throughput macromolecular crystallography. Here, the de novo automated crystal structure determination at 1.28 A resolution of an NAD(P)H-dependent FMN reductase flavoprotein from Pseudomonas aeruginosa PA01-derived protein Q9I4D4 using the anomalous signal from an unusually small number of S atoms is reported. Although this protein lacks the flavodoxin key fingerprint motif [(T/S)XTGXT], it has been confirmed to bind flavin mononucleotide and the binding site was identified via X-ray crystallography. This protein contains a novel flavin mononucleotide-binding site GSLRSGSYN, which has not been previously reported. Detailed statistics pertaining to sulfur phasing and other factors contributing to structure determination are discussed. Structural comparisons of the apoenzyme and the protein complexed with flavin mononucleotide show conformational changes on cofactor binding. NADPH-dependent activity has been confirmed with biochemical assays.

About this Structure

1RTT is a Single protein structure of sequence from Pseudomonas aeruginosa pao1 with as ligand. Full crystallographic information is available from OCA.

Reference

Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal., Agarwal R, Bonanno JB, Burley SK, Swaminathan S, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):383-91. Epub 2006, Mar 18. PMID:16552139

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