1t1e: Difference between revisions
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|PDB= 1t1e |SIZE=350|CAPTION= <scene name='initialview01'>1t1e</scene>, resolution 1.18Å | |PDB= 1t1e |SIZE=350|CAPTION= <scene name='initialview01'>1t1e</scene>, resolution 1.18Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= KSCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | |GENE= KSCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1gt9|1GT9]], [[1gtg|1GTG]], [[1gtj|1GTJ]], [[1gtl|1GTL]], [[1t1g|1T1G]], [[1t1i|1T1I]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1e OCA], [http://www.ebi.ac.uk/pdbsum/1t1e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t1e RCSB]</span> | |||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
1T1E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | 1T1E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1E OCA]. | ||
==Reference== | ==Reference== | ||
1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase., Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W, Structure. 2004 Jul;12(7):1313-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15242607 15242607] | 1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase., Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W, Structure. 2004 Jul;12(7):1313-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15242607 15242607] | ||
[[Category: | [[Category: Bacteria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
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[[Category: Oda, K.]] | [[Category: Oda, K.]] | ||
[[Category: Oyama, H.]] | [[Category: Oyama, H.]] | ||
[[Category: activation mechanism]] | [[Category: activation mechanism]] | ||
[[Category: proenzyme]] | [[Category: proenzyme]] | ||
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[[Category: serine-carboxyl proteinase]] | [[Category: serine-carboxyl proteinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:51 2008'' | ||
Revision as of 23:49, 30 March 2008
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| , resolution 1.18Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | KSCP (Bacteria) | ||||||
| Related: | 1GT9, 1GTG, 1GTJ, 1GTL, 1T1G, 1T1I
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)
OverviewOverview
Kumamolisin, an extracellular proteinase derived from an acido/thermophilic Bacillus, belongs to the sedolisin family of endopeptidases characterized by a subtilisin-like fold and a Ser-Glu-Asp catalytic triad. In kumamolisin, the Asp82 carboxylate hydrogen bonds to Glu32-Trp129, which might act as a proton sink stabilizing the catalytic residues. The 1.2/1.3 A crystal structures of the Glu32-->Ala and Trp129-->Ala mutants show that both mutations affect the active-site conformation, causing a 95% activity decrease. In addition, the 1.2 A crystal structure of the Ser278-->Ala mutant of pro-kumamolisin was determined. The prodomain exhibits a half-beta sandwich core docking to the catalytic domain similarly as the equivalent subtilisin prodomains in their catalytic-domain complexes. This pro-kumamolisin structure displays, for the first time, the uncleaved linker segment running across the active site and connecting the prodomain with the properly folded catalytic domain. The structure strongly points to an initial intramolecular activation cleavage in subtilases, as presumed for pro-subtilisin and pro-furin.
About this StructureAbout this Structure
1T1E is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
ReferenceReference
1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase., Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W, Structure. 2004 Jul;12(7):1313-23. PMID:15242607
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