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| [[Image:1rh9.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1rh9| PDB=1rh9 | SCENE= }} | | {{STRUCTURE_1rh9| PDB=1rh9 | SCENE= }} |
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| '''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''
| | ===Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)=== |
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| ==Overview==
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| 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 line below this paragraph, {{ABSTRACT_PUBMED_15840830}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15840830 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15840830}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mannan]] | | [[Category: Mannan]] |
| [[Category: Retaining]] | | [[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 Sun Jul 27 18:30:20 2008'' |
