1nqd: Difference between revisions
New page: left|200px<br /><applet load="1nqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nqd, resolution 1.65Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1nqd.jpg|left|200px]]<br /><applet load="1nqd" size=" | [[Image:1nqd.jpg|left|200px]]<br /><applet load="1nqd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nqd, resolution 1.65Å" /> | caption="1nqd, resolution 1.65Å" /> | ||
'''CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.65 ANGSTROM RESOLUTION IN PRESENCE OF CALCIUM'''<br /> | '''CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.65 ANGSTROM RESOLUTION IN PRESENCE OF CALCIUM'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of a collagen-binding domain (CBD) with an | The crystal structure of a collagen-binding domain (CBD) with an N-terminal domain linker from Clostridium histolyticum class I collagenase was determined at 1.00 A resolution in the absence of calcium (1NQJ) and at 1.65 A resolution in the presence of calcium (1NQD). The mature enzyme is composed of four domains: a metalloprotease domain, a spacing domain and two CBDs. A 12-residue-long linker is found at the N-terminus of each CBD. In the absence of calcium, the CBD reveals a beta-sheet sandwich fold with the linker adopting an alpha-helix. The addition of calcium unwinds the linker and anchors it to the distal side of the sandwich as a new beta-strand. The conformational change of the linker upon calcium binding is confirmed by changes in the Stokes and hydrodynamic radii as measured by size exclusion chromatography and by dynamic light scattering with and without calcium. Furthermore, extensive mutagenesis of conserved surface residues and collagen-binding studies allow us to identify the collagen-binding surface of the protein and propose likely collagen-protein binding models. | ||
==About this Structure== | ==About this Structure== | ||
1NQD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_histolyticum Clostridium histolyticum] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Microbial_collagenase Microbial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.3 3.4.24.3] Full crystallographic information is available from [http:// | 1NQD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_histolyticum Clostridium histolyticum] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Microbial_collagenase Microbial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.3 3.4.24.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Okabe, A.]] | [[Category: Okabe, A.]] | ||
[[Category: Sakon, J.]] | [[Category: Sakon, J.]] | ||
[[Category: Wilson, J | [[Category: Wilson, J J.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:53 2008'' | ||
Revision as of 15:08, 21 February 2008
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CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.65 ANGSTROM RESOLUTION IN PRESENCE OF CALCIUM
OverviewOverview
The crystal structure of a collagen-binding domain (CBD) with an N-terminal domain linker from Clostridium histolyticum class I collagenase was determined at 1.00 A resolution in the absence of calcium (1NQJ) and at 1.65 A resolution in the presence of calcium (1NQD). The mature enzyme is composed of four domains: a metalloprotease domain, a spacing domain and two CBDs. A 12-residue-long linker is found at the N-terminus of each CBD. In the absence of calcium, the CBD reveals a beta-sheet sandwich fold with the linker adopting an alpha-helix. The addition of calcium unwinds the linker and anchors it to the distal side of the sandwich as a new beta-strand. The conformational change of the linker upon calcium binding is confirmed by changes in the Stokes and hydrodynamic radii as measured by size exclusion chromatography and by dynamic light scattering with and without calcium. Furthermore, extensive mutagenesis of conserved surface residues and collagen-binding studies allow us to identify the collagen-binding surface of the protein and propose likely collagen-protein binding models.
About this StructureAbout this Structure
1NQD is a Single protein structure of sequence from Clostridium histolyticum with as ligand. Active as Microbial collagenase, with EC number 3.4.24.3 Full crystallographic information is available from OCA.
ReferenceReference
A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation., Wilson JJ, Matsushita O, Okabe A, Sakon J, EMBO J. 2003 Apr 15;22(8):1743-52. PMID:12682007
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