1bhu: Difference between revisions

Revision as of 12:55, 21 February 2008

THE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR, SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS TK-23, NMR, MINIMIZED AVERAGE STRUCTURE

OverviewOverview

The Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23, is a proteinaceous metalloproteinase inhibitor, and consists of 102 amino acid residues with two disulfide bridges. SMPI specifically inhibits metalloproteinases such as thermolysin. In the present work, the solution structure of SMPI was determined on the basis of 1536 nuclear Overhauser enhancement derived distance restraints and 52 dihedral angle restraints obtained from three-bond spin coupling constants. The final ensemble of 20 NMR structures overlaid onto their mean coordinate with backbone (N, Calpha, C') r.m.s.d. values of 0. 45(+/-0.11) A and 0.57(+/-0.18) A for residues 6 to 99 and the entire 102 residues, respectively. SMPI is essentially composed of two beta-sheets, each consisting of four antiparallel beta-strands. The structure can be considered as two Greek key motifs with 2-fold internal symmetry, a Greek key beta-barrel. One unique structural feature found in SMPI is in its extension between the first and second strands of the second Greek key motif. Interestingly, this extended segment is known to be involved in the inhibitory activity of SMPI. In the absence of sequence similarity, the SMPI structure shows clear similarity to both domains of the eye lens crystallins, both domains of the calcium sensor protein-S, as well as the single-domain yeast killer toxin. The yeast killer toxin structure was thought to be a precursor of the two-domain beta gamma-crystallin proteins, because of its structural similarity to each domain of the beta gamma-crystallins. SMPI thus provides another example of a single-domain protein structure that corresponds to the ancestral fold from which the two-domain proteins in the beta gamma-crystallin superfamily are believed to have evolved.

About this StructureAbout this Structure

1BHU is a Single protein structure of sequence from Streptomyces nigrescens. Full crystallographic information is available from OCA.

ReferenceReference

NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure., Ohno A, Tate S, Seeram SS, Hiraga K, Swindells MB, Oda K, Kainosho M, J Mol Biol. 1998 Sep 18;282(2):421-33. PMID:9735297

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1bhu.gif|left|200px]]<br /><applet load="1bhu" size="450" color="white" frame="true" align="right" spinBox="true"
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 '''THE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR, SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS TK-23, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
 ==Overview==
-The Streptomyces metalloproteinase inhibitor, SMPI, isolated from, Streptomyces nigrescens TK-23, is a proteinaceous metalloproteinase, inhibitor, and consists of 102 amino acid residues with two disulfide, bridges. SMPI specifically inhibits metalloproteinases such as, thermolysin. In the present work, the solution structure of SMPI was, determined on the basis of 1536 nuclear Overhauser enhancement derived, distance restraints and 52 dihedral angle restraints obtained from, three-bond spin coupling constants. The final ensemble of 20 NMR, structures overlaid onto their mean coordinate with backbone (N, Calpha, C') r.m.s.d. values of 0. 45(+/-0.11) A and 0.57(+/-0.18) A for residues 6, to 99 and the entire 102 residues, respectively. SMPI is essentially, composed of two beta-sheets, each consisting of four antiparallel, beta-strands. The structure can be considered as two Greek key motifs with, 2-fold internal symmetry, a Greek key beta-barrel. One unique structural, feature found in SMPI is in its extension between the first and second, strands of the second Greek key motif. Interestingly, this extended, segment is known to be involved in the inhibitory activity of SMPI. In the, absence of sequence similarity, the SMPI structure shows clear similarity, to both domains of the eye lens crystallins, both domains of the calcium, sensor protein-S, as well as the single-domain yeast killer toxin. The, yeast killer toxin structure was thought to be a precursor of the, two-domain beta gamma-crystallin proteins, because of its structural, similarity to each domain of the beta gamma-crystallins. SMPI thus, provides another example of a single-domain protein structure that, corresponds to the ancestral fold from which the two-domain proteins in, the beta gamma-crystallin superfamily are believed to have evolved.
+The Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23, is a proteinaceous metalloproteinase inhibitor, and consists of 102 amino acid residues with two disulfide bridges. SMPI specifically inhibits metalloproteinases such as thermolysin. In the present work, the solution structure of SMPI was determined on the basis of 1536 nuclear Overhauser enhancement derived distance restraints and 52 dihedral angle restraints obtained from three-bond spin coupling constants. The final ensemble of 20 NMR structures overlaid onto their mean coordinate with backbone (N, Calpha, C') r.m.s.d. values of 0. 45(+/-0.11) A and 0.57(+/-0.18) A for residues 6 to 99 and the entire 102 residues, respectively. SMPI is essentially composed of two beta-sheets, each consisting of four antiparallel beta-strands. The structure can be considered as two Greek key motifs with 2-fold internal symmetry, a Greek key beta-barrel. One unique structural feature found in SMPI is in its extension between the first and second strands of the second Greek key motif. Interestingly, this extended segment is known to be involved in the inhibitory activity of SMPI. In the absence of sequence similarity, the SMPI structure shows clear similarity to both domains of the eye lens crystallins, both domains of the calcium sensor protein-S, as well as the single-domain yeast killer toxin. The yeast killer toxin structure was thought to be a precursor of the two-domain beta gamma-crystallin proteins, because of its structural similarity to each domain of the beta gamma-crystallins. SMPI thus provides another example of a single-domain protein structure that corresponds to the ancestral fold from which the two-domain proteins in the beta gamma-crystallin superfamily are believed to have evolved.
 ==About this Structure==
-BHU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_nigrescens Streptomyces nigrescens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BHU OCA].
+BHU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_nigrescens Streptomyces nigrescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHU OCA].
 ==Reference==
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 [[Category: Oda, K.]]
 [[Category: Ohno, A.]]
-[[Category: Seeram, S.S.]]
+[[Category: Seeram, S S.]]
 [[Category: Tate, S.]]
 [[Category: metalloproteinase inhibitor]]
 [[Category: signal]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:39:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:27 2008''