Related ArticlesSolution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the conversion of phenol and some of its methyl-substituted derivatives to catechol. In addition to a reductase component which transfers electrons from NADH, optimal turnover of the hydroxylase requires P2, a protein containing 90 amino acids which is readily resolved from the other components. The three-dimensional solution structure of P2 has been solved by 3D heteronuclear NMR spectroscopy. On the basis of 1206 experimental constraints, including 1060 distance constraints obtained from NOEs, 70 phi dihedral angle constraints, 42 psi dihedral angle constraints, and 34 hydrogen bond constraints, a total of 12 converged structures were obtained. The atomic root mean square deviation for the 12 converged structure with respect to the mean coordinates is 2.48 A for the backbone atoms and 3.85 A for all the heavy atoms. This relatively large uncertainty can be ascribed to conformational flexibility and exchange. The molecular structure of P2 is composed of three helices, six antiparallel beta-strands, one beta-hairpin, and some less ordered regions. This is the first structure among the known multicomponent oxygenases. On the basis of the three-dimensional structure of P2, sequence comparisons with similar proteins from other multicomponent oxygenases suggested that all of these proteins may have a conserved structure in the core regions.
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
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J Am Chem Soc. 2010 Aug 20;
Authors: Hu Y, Zhao E, Li H, Xia B, Jin C
The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive...
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[NMR paper] Solution structure of phenol hydroxylase protein component P2 determined by NMR spect
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the...
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[NMR paper] The solution structure of bovine ferricytochrome b5 determined using heteronuclear NM
The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods.
J Mol Biol. 1996 Apr 26;258(1):172-89
Authors: Muskett FW, Kelly GP, Whitford D
The solution structure of a recombinant form of cytochrome b5 containing 104 amino acid residues has been determined using three-dimensional NMR...
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[NMR paper] Solution structure of the B-chain of insulin as determined by 1H NMR spectroscopy. Co
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Int J Pept Protein Res. 1995 Nov;46(5):424-33
Authors: Hawkins B, Cross K, Craik D
The solution structure of the isolated B-chain of...
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[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
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Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
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[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
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Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
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[NMR paper] Solution structure of component B from methane monooxygenase derived through heteronu
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
Biochemistry. 1999 May 4;38(18):5799-812
Authors: Chang SL, Wallar BJ, Lipscomb JD, Mayo KH
Methane monooxygenase (MMO) is a nonheme iron-containing enzyme which consists of three protein components: a...
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Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis
Yunfei Hu et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1053785/aop/images/medium/ja-2010-053785_0001.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society