1llo

From Proteopedia

(Difference between revisions)

Revision as of 06:46, 18 August 2021

HEVAMINE A (A PLANT ENDOCHITINASE/LYSOZYME) COMPLEXED WITH ALLOSAMIDIN

Structural highlights

1llo is a 1 chain structure with sequence from Hevea brasiliensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CHLY_HEVBR] Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow.

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 plant enzyme hevamine has both chitinase and lysozyme activity. HPLC analysis of the products of the hydrolysis of chitopentaose shows that hevamine acts with retention of the configuration, despite the absence of a nucleophilic or stabilizing carboxylate. To analyze the stabilization of a putative oxocarbonium ion intermediate, the X-ray structure of hevamine complexed with the inhibitor allosamidin was determined at 1.85 A resolution. This structure supports the role of Glu127 as a proton donor. The allosamizoline group binds in the center of the active site, mimicking a reaction intermediate in which a positive charge at C1 is stabilized intramolecularly by the carbonyl oxygen of the N-acetyl group at C2.

Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis.,Terwisscha van Scheltinga AC, Armand S, Kalk KH, Isogai A, Henrissat B, Dijkstra BW Biochemistry. 1995 Dec 5;34(48):15619-23. PMID:7495789^[1]

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

References

↑ Terwisscha van Scheltinga AC, Armand S, Kalk KH, Isogai A, Henrissat B, Dijkstra BW. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry. 1995 Dec 5;34(48):15619-23. PMID:7495789

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1llo"

@@ Line 3: / Line 3: @@
 <StructureSection load='1llo' size='340' side='right'caption='[[1llo]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1llo]] is a 1 chain structure with 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=1LLO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LLO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1llo]] 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=1LLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMI:ALLOSAMIZOLINE'>AMI</scene>, <scene name='pdbligand=NAA:N-ACETYL-D-ALLOSAMINE'>NAA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMI:ALLOSAMIZOLINE'>AMI</scene>, <scene name='pdbligand=NAA:N-ACETYL-D-ALLOSAMINE'>NAA</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1llo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llo OCA], [http://pdbe.org/1llo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1llo RCSB], [http://www.ebi.ac.uk/pdbsum/1llo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1llo ProSAT]</span></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=1llo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llo OCA], [https://pdbe.org/1llo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llo RCSB], [https://www.ebi.ac.uk/pdbsum/1llo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1llo

From Proteopedia

Revision as of 06:46, 18 August 2021

HEVAMINE A (A PLANT ENDOCHITINASE/LYSOZYME) COMPLEXED WITH ALLOSAMIDIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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