1rh9: Difference between revisions

Revision as of 18:30, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rh9.png

Template:STRUCTURE 1rh9

Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)

Template:ABSTRACT PUBMED 15840830

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 Sun Jul 27 18:30:20 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1rh9.gif|left|200px]]
+{{Seed}}
+[[Image:1rh9.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1rh9|  PDB=1rh9  |  SCENE=  }}
-'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''
+===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.
+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.
+-->
+{{ABSTRACT_PUBMED_15840830}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Mannan]]
 [[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''