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1hvq

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[[Image:1hvq.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR==
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|PDB= 1hvq |SIZE=350|CAPTION= <scene name='initialview01'>1hvq</scene>, resolution 2.2&Aring;
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<StructureSection load='1hvq' size='340' side='right'caption='[[1hvq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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<table><tr><td colspan='2'>[[1hvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HVQ FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hvq OCA], [https://pdbe.org/1hvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hvq RCSB], [https://www.ebi.ac.uk/pdbsum/1hvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hvq ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hvq OCA], [http://www.ebi.ac.uk/pdbsum/1hvq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hvq RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CHLY_HEVBR CHLY_HEVBR] Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow.
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== Evolutionary Conservation ==
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'''CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hv/1hvq_consurf.spt"</scriptWhenChecked>
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BACKGROUND: Hevamine is a member of one of several families of plant chitinases and lysozymes that are important for plant defence against pathogenic bacteria and fungi. The enzyme can hydrolyze the linear polysaccharide chains of chitin and peptidoglycan. A full understanding of the structure/function relationships of chitinases might facilitate the production of transgenic plants with increased resistance towards a wide range of pathogens. RESULTS: The crystal structure of hevamine has been determined to a resolution of 2.2 A, and refined to an R-factor of 0.169. The enzyme possesses a (beta alpha)8-barrel fold. An inhibitor binding study shows that the substrate-binding cleft is located at the carboxy-terminal end of the beta-barrel, near the conserved Glu127. Glu127 is in a position to act as the catalytic proton donor, but no residue that might stabilize a positively charged oxocarbonium ion intermediate was found. A likely mechanism of substrate hydrolysis is by direct attack of a water molecule on the C1 atom of the scissile bond, resulting in inversion of the configuration at C1. CONCLUSIONS: The structure of hevamine shows a completely new lysozyme/chitinase fold and represents a new class of polysaccharide-hydrolyzing (beta alpha)8-barrel enzymes. Because the residues conserved in the family to which hevamine belongs are important for maintaining the structure of the (beta alpha)8-barrel, all members of the family, including fungal, bacterial and insect chitinases, are likely to share this architecture. The crystal structure obtained provides a basis for protein engineering studies in this family of chitinases.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1HVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVQ OCA].
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</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=1hvq ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor., Terwisscha van Scheltinga AC, Kalk KH, Beintema JJ, Dijkstra BW, Structure. 1994 Dec 15;2(12):1181-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7704528 7704528]
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</StructureSection>
[[Category: Hevea brasiliensis]]
[[Category: Hevea brasiliensis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Beintema, J J.]]
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[[Category: Beintema JJ]]
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[[Category: Dijkstra, B W.]]
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[[Category: Dijkstra BW]]
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[[Category: Kalk, K H.]]
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[[Category: Kalk KH]]
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[[Category: Scheltinga, A C.Terwisscha Van.]]
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[[Category: Terwisscha Van Scheltinga AC]]
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[[Category: chitin degradation]]
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[[Category: glycosidase]]
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[[Category: multifunctional enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:05 2008''
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Current revision

CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR

PDB ID 1hvq

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