1gtj: Difference between revisions

Line 1:

[[Image:1gtj.~~gif~~|left|200px]]

[[Image:1gtj.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO~~'''~~

===CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO===

~~==Overview==~~

<!--

~~Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN~~-~~32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine~~-~~carboxyl proteinases~~, ~~which also includes CLN2~~, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.~~4 A resolution~~. ~~As its Pseudomonas homolog~~, ~~kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling~~ the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature.

The line below this paragraph, {{ABSTRACT_PUBMED_12057200}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12057200 is the PubMed ID number.

-->

==About this Structure==

Line 33:

Line 37:

[[Category: Serine-carboxyl type proteinase]]

[[Category: Thermostable]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 17~~:59:25 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:03:15 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1gtj.gif|left|200px]]
+{{Seed}}
+[[Image:1gtj.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1gtj|  PDB=1gtj  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO'''
+===CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO===
-==Overview==
+<!--
-Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine-carboxyl proteinases, which also includes CLN2, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature.
+The line below this paragraph, {{ABSTRACT_PUBMED_12057200}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12057200 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12057200}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Serine-carboxyl type proteinase]]
 [[Category: Thermostable]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:59:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:03:15 2008''