1bhe: Difference between revisions

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

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

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~~'''~~POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA~~'''~~

===POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA===

~~==Overview==~~

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The ~~crystal structure of~~ the ~~40-kDa endo-polygalacturonase from Erwinia carotovora ssp. carotovora was solved by multiple isomorphous replacement and refined at 1.9 A~~ to ~~a conventional crystallographic R-factor of 0.198 and Rfree of 0.239. This is~~ the ~~first structure of a polygalacturonase and comprises a 10 turn right-handed parallel beta-helix domain with two loop regions forming a "tunnel like" substrate-binding cleft~~. Sequence conservation indicates that the active site of polygalacturonase is between these two loop regions, and comparison of the structure of polygalacturonase with that of rhamnogalacturonase A from Aspergillus aculeatus enables two conserved aspartates, presumed to be catalytic residues, to be identified. ~~An adjacent histidine, in accord with biochemical results~~, is ~~also seen~~. ~~A similarity in overall electrostatic properties of the substrate~~-~~binding clefts of polygalacturonase and pectate lyase, which bind and cleave the same substrate, polygalacturonic acid, is also revealed.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9733763}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9733763 is the PubMed ID number.

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==About this Structure==

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[[Category: Glycosidase]]

[[Category: Hydrolyses polygalacturonic acid]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:30:59 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:10:18 2008''

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-[[Image:1bhe.gif|left|200px]]
+{{Seed}}
+[[Image:1bhe.png|left|200px]]
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 {{STRUCTURE_1bhe|  PDB=1bhe  |  SCENE=  }}
-'''POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA'''
+===POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA===
-==Overview==
+<!--
-The crystal structure of the 40-kDa endo-polygalacturonase from Erwinia carotovora ssp. carotovora was solved by multiple isomorphous replacement and refined at 1.9 A to a conventional crystallographic R-factor of 0.198 and Rfree of 0.239. This is the first structure of a polygalacturonase and comprises a 10 turn right-handed parallel beta-helix domain with two loop regions forming a "tunnel like" substrate-binding cleft. Sequence conservation indicates that the active site of polygalacturonase is between these two loop regions, and comparison of the structure of polygalacturonase with that of rhamnogalacturonase A from Aspergillus aculeatus enables two conserved aspartates, presumed to be catalytic residues, to be identified. An adjacent histidine, in accord with biochemical results, is also seen. A similarity in overall electrostatic properties of the substrate-binding clefts of polygalacturonase and pectate lyase, which bind and cleave the same substrate, polygalacturonic acid, is also revealed.
+The line below this paragraph, {{ABSTRACT_PUBMED_9733763}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9733763 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9733763}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Glycosidase]]
 [[Category: Hydrolyses polygalacturonic acid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:30:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:10:18 2008''