1rh9
From Proteopedia
(New page: 200px<br /><applet load="1rh9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rh9, resolution 1.50Å" /> '''Family GH5 endo-beta...) |
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| - | [[Image:1rh9.gif|left|200px]]<br /><applet load="1rh9" size=" | + | [[Image:1rh9.gif|left|200px]]<br /><applet load="1rh9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rh9, resolution 1.50Å" /> | caption="1rh9, resolution 1.50Å" /> | ||
'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''<br /> | '''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional crystal structure of tomato (Lycopersicon | + | The three-dimensional crystal structure of tomato (Lycopersicon esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A resolution. The enzyme adopts the (beta/alpha)(8) fold common to the members of glycohydrolase family GH5. The structure is comparable with those of the homologous Trichoderma reesei and Thermomonospora fusca beta-mannanases: There is a conserved three-stranded beta-sheet located near the N terminus that stacks against the central beta-barrel at the end opposite the active site. Three noncanonical beta-helices surround the active site. Similar helices are found in T. reesei but not T. fusca beta-mannanase. By analogy with other beta-mannanases, the catalytic acid/base residue is E204 and the nucleophile residue is E318. The active site cleft of L. esculentum beta-mannanase most closely resembles that of the T. reesei isozyme. A model of substrate binding in LeMAN4a is proposed in which the mannosyl residue occupying the -1 subsite of the enzyme adopts the (1)S(5) skew-boat conformation. |
==About this Structure== | ==About this Structure== | ||
| - | 1RH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Active as [http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] Full crystallographic information is available from [http:// | + | 1RH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Active as [http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Solanum lycopersicum]] | [[Category: Solanum lycopersicum]] | ||
| - | [[Category: Bewley, J | + | [[Category: Bewley, J D.]] |
[[Category: Bourgault, R.]] | [[Category: Bourgault, R.]] | ||
| - | [[Category: Oakley, A | + | [[Category: Oakley, A J.]] |
| - | [[Category: Wilce, M | + | [[Category: Wilce, M C.J.]] |
[[Category: endo-beta-mannase]] | [[Category: endo-beta-mannase]] | ||
[[Category: glycoside hydrolase family 5]] | [[Category: glycoside hydrolase family 5]] | ||
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[[Category: retaining]] | [[Category: retaining]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:53 2008'' |
Revision as of 12:51, 21 February 2008
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Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)
Overview
The three-dimensional crystal structure of tomato (Lycopersicon esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A resolution. The enzyme adopts the (beta/alpha)(8) fold common to the members of glycohydrolase family GH5. The structure is comparable with those of the homologous Trichoderma reesei and Thermomonospora fusca beta-mannanases: There is a conserved three-stranded beta-sheet located near the N terminus that stacks against the central beta-barrel at the end opposite the active site. Three noncanonical beta-helices surround the active site. Similar helices are found in T. reesei but not T. fusca beta-mannanase. By analogy with other beta-mannanases, the catalytic acid/base residue is E204 and the nucleophile residue is E318. The active site cleft of L. esculentum beta-mannanase most closely resembles that of the T. reesei isozyme. A model of substrate binding in LeMAN4a is proposed in which the mannosyl residue occupying the -1 subsite of the enzyme adopts the (1)S(5) skew-boat conformation.
About this Structure
1RH9 is a Single protein structure of sequence from Solanum lycopersicum. Active as Mannan endo-1,4-beta-mannosidase, with EC number 3.2.1.78 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit., Bourgault R, Oakley AJ, Bewley JD, Wilce MC, Protein Sci. 2005 May;14(5):1233-41. PMID:15840830
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