1bhu: Difference between revisions
No edit summary |
No edit summary |
||
| (13 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==THE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR, SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS TK-23, NMR, MINIMIZED AVERAGE STRUCTURE== | |||
<StructureSection load='1bhu' size='340' side='right'caption='[[1bhu]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1bhu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_nigrescens Streptomyces nigrescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHU FirstGlance]. <br> | |||
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhu OCA], [https://pdbe.org/1bhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bhu RCSB], [https://www.ebi.ac.uk/pdbsum/1bhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bhu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IMEP_STRNI IMEP_STRNI] Inhibits microbial metallo-proteinases, such as thermolysin, but not serine, thiol, or carboxyl proteinases. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
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. | ||
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<ref>PMID:9735297</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1bhu" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces nigrescens]] | [[Category: Streptomyces nigrescens]] | ||
[[Category: Hiraga | [[Category: Hiraga K]] | ||
[[Category: Kainosho | [[Category: Kainosho M]] | ||
[[Category: Oda | [[Category: Oda K]] | ||
[[Category: Ohno | [[Category: Ohno A]] | ||
[[Category: Seeram | [[Category: Seeram SS]] | ||
[[Category: Tate | [[Category: Tate S]] | ||
Latest revision as of 10:17, 23 October 2024
THE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR, SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS TK-23, NMR, MINIMIZED AVERAGE STRUCTURETHE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR, SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS TK-23, NMR, MINIMIZED AVERAGE STRUCTURE
Structural highlights
FunctionIMEP_STRNI Inhibits microbial metallo-proteinases, such as thermolysin, but not serine, thiol, or carboxyl proteinases. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||