1rh9: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rh9.gif|left|200px]]<br /><applet load="1rh9" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rh9, resolution 1.50&Aring;" />
caption="1rh9, resolution 1.50&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RH9 OCA].  
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.D.]]
[[Category: Bewley, J D.]]
[[Category: Bourgault, R.]]
[[Category: Bourgault, R.]]
[[Category: Oakley, A.J.]]
[[Category: Oakley, A J.]]
[[Category: Wilce, M.C.J.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:35:53 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:53 2008''