1llo
From Proteopedia
(New page: 200px<br /><applet load="1llo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1llo, resolution 1.85Å" /> '''HEVAMINE A (A PLANT ...) |
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| - | [[Image:1llo.gif|left|200px]]<br /><applet load="1llo" size=" | + | [[Image:1llo.gif|left|200px]]<br /><applet load="1llo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1llo, resolution 1.85Å" /> | caption="1llo, resolution 1.85Å" /> | ||
'''HEVAMINE A (A PLANT ENDOCHITINASE/LYSOZYME) COMPLEXED WITH ALLOSAMIDIN'''<br /> | '''HEVAMINE A (A PLANT ENDOCHITINASE/LYSOZYME) COMPLEXED WITH ALLOSAMIDIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The plant enzyme hevamine has both chitinase and lysozyme activity. HPLC | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1LLO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis] with AMI as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LLO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis] with <scene name='pdbligand=AMI:'>AMI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Armand, S.]] | [[Category: Armand, S.]] | ||
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
[[Category: Henrissat, B.]] | [[Category: Henrissat, B.]] | ||
[[Category: Isogai, A.]] | [[Category: Isogai, A.]] | ||
| - | [[Category: Kalk, K | + | [[Category: Kalk, K H.]] |
| - | [[Category: Scheltinga, A | + | [[Category: Scheltinga, A C.Terwisscha Van.]] |
[[Category: AMI]] | [[Category: AMI]] | ||
[[Category: chitinase]] | [[Category: chitinase]] | ||
[[Category: lysozyme]] | [[Category: lysozyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:06 2008'' |
Revision as of 11:46, 21 February 2008
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HEVAMINE A (A PLANT ENDOCHITINASE/LYSOZYME) COMPLEXED WITH ALLOSAMIDIN
Overview
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.
About this Structure
1LLO is a Single protein structure of sequence from Hevea brasiliensis with as ligand. Full crystallographic information is available from OCA.
Reference
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
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