1rh9: Difference between revisions

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[[Image:1rh9.gif|left|200px]]
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{{STRUCTURE_1rh9|  PDB=1rh9  |  SCENE=  }}
'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''


==Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)==
<StructureSection load='1rh9' size='340' side='right'caption='[[1rh9]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
</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/initialview03.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.


==Overview==
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>
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''

Latest revision as of 10:19, 30 October 2024

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

Structural highlights

1rh9 is a 1 chain structure with sequence from Solanum lycopersicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAN4_SOLLC Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Bourgault R, Bewley JD. Variation in its C-terminal amino acids determines whether endo-beta-mannanase is active or inactive in ripening tomato fruits of different cultivars. Plant Physiol. 2002 Nov;130(3):1254-62. PMID:12427992 doi:http://dx.doi.org/10.1104/pp.011890
  2. ↑ Schroder R, Wegrzyn TF, Sharma NN, Atkinson RG. LeMAN4 endo-beta-mannanase from ripe tomato fruit can act as a mannan transglycosylase or hydrolase. Planta. 2006 Oct;224(5):1091-102. Epub 2006 Apr 29. PMID:16649044 doi:http://dx.doi.org/10.1007/s00425-006-0286-0
  3. ↑ Bourgault R, Oakley AJ, Bewley JD, Wilce MC. Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit. Protein Sci. 2005 May;14(5):1233-41. PMID:15840830 doi:14/5/1233

1rh9, resolution 1.50Å

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