This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1rh9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:24, 25 October 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1rh9.gif|left|200px]]
 
-
<!--
+
==Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)==
-
The line below this paragraph, containing "STRUCTURE_1rh9", creates the "Structure Box" on the page.
+
<StructureSection load='1rh9' size='340' side='right'caption='[[1rh9]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1rh9]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RH9 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-
-->
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh9 OCA], [https://pdbe.org/1rh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh9 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh9 ProSAT]</span></td></tr>
-
{{STRUCTURE_1rh9| PDB=1rh9 | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MAN4_SOLLC MAN4_SOLLC] Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening.<ref>PMID:12427992</ref> <ref>PMID:16649044</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rh/1rh9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rh9 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''
+
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<ref>PMID:15840830</ref>
-
 
+
-
 
+
-
==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==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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].
+
</div>
 +
<div class="pdbe-citations 1rh9" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
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]
+
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
-
[[Category: Mannan endo-1,4-beta-mannosidase]]
+
== References ==
-
[[Category: Single protein]]
+
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Solanum lycopersicum]]
[[Category: Solanum lycopersicum]]
-
[[Category: Bewley, J D.]]
+
[[Category: Bewley JD]]
-
[[Category: Bourgault, R.]]
+
[[Category: Bourgault R]]
-
[[Category: Oakley, A J.]]
+
[[Category: Oakley AJ]]
-
[[Category: Wilce, M C.J.]]
+
[[Category: Wilce MCJ]]
-
[[Category: Endo-beta-mannase]]
+
-
[[Category: Glycoside hydrolase family 5]]
+
-
[[Category: Mannan]]
+
-
[[Category: Retaining]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:29:50 2008''
+

Current revision

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

PDB ID 1rh9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rh9"
Personal tools