1rh9: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1rh9.gif|left|200px]] | [[Image:1rh9.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1rh9", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1rh9| PDB=1rh9 | SCENE= }} | |||
}} | |||
'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)''' | '''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)''' | ||
Line 30: | Line 27: | ||
[[Category: Oakley, A J.]] | [[Category: Oakley, A J.]] | ||
[[Category: Wilce, M C.J.]] | [[Category: Wilce, M C.J.]] | ||
[[Category: | [[Category: Endo-beta-mannase]] | ||
[[Category: | [[Category: Glycoside hydrolase family 5]] | ||
[[Category: | [[Category: Mannan]] | ||
[[Category: | [[Category: Retaining]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:29:50 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 07:29, 3 May 2008
Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)
OverviewOverview
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 StructureAbout this Structure
1RH9 is a Single protein structure of sequence from Solanum lycopersicum. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 07:29:50 2008