1bhe
From Proteopedia
(New page: 200px<br /><applet load="1bhe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhe, resolution 1.9Å" /> '''POLYGALACTURONASE FRO...) |
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| - | [[Image:1bhe.gif|left|200px]]<br /><applet load="1bhe" size=" | + | [[Image:1bhe.gif|left|200px]]<br /><applet load="1bhe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bhe, resolution 1.9Å" /> | caption="1bhe, resolution 1.9Å" /> | ||
'''POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA'''<br /> | '''POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the 40-kDa endo-polygalacturonase from Erwinia | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1BHE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Active as [http://en.wikipedia.org/wiki/Polygalacturonase Polygalacturonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.15 3.2.1.15] Full crystallographic information is available from [http:// | + | 1BHE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Active as [http://en.wikipedia.org/wiki/Polygalacturonase Polygalacturonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.15 3.2.1.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolyses polygalacturonic acid]] | [[Category: hydrolyses polygalacturonic acid]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:20 2008'' |
Revision as of 09:55, 21 February 2008
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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.
About this Structure
1BHE is a Single protein structure of sequence from Pectobacterium carotovorum. Active as Polygalacturonase, with EC number 3.2.1.15 Full crystallographic information is available from OCA.
Reference
Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora., Pickersgill R, Smith D, Worboys K, Jenkins J, J Biol Chem. 1998 Sep 18;273(38):24660-4. PMID:9733763
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