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1rh9

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[[Image:1rh9.gif|left|200px]]<br /><applet load="1rh9" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rh9.gif|left|200px]]
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caption="1rh9, resolution 1.50&Aring;" />
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'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''<br />
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{{Structure
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|PDB= 1rh9 |SIZE=350|CAPTION= <scene name='initialview01'>1rh9</scene>, resolution 1.50&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE= LeMAN4a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4081 Solanum lycopersicum])
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}}
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'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1RH9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH9 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15840830 15840830]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15840830 15840830]
[[Category: Mannan endo-1,4-beta-mannosidase]]
[[Category: Mannan endo-1,4-beta-mannosidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: retaining]]
[[Category: retaining]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:36 2008''

Revision as of 11:51, 20 March 2008


PDB ID 1rh9

Drag the structure with the mouse to rotate
, resolution 1.50Å
Gene: LeMAN4a (Solanum lycopersicum)
Activity: Mannan endo-1,4-beta-mannosidase, with EC number 3.2.1.78
Coordinates: save as pdb, mmCIF, xml



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. 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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