Chitinase
From Proteopedia
(Difference between revisions)
												
			
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**[[3g6l]] - BoChi residues 21-426 – ''Bionectria ochroleuca''<br />  | **[[3g6l]] - BoChi residues 21-426 – ''Bionectria ochroleuca''<br />  | ||
**[[3oa5]], [[4dws]] – Chi – ''Yersinia entomophaga''<br />  | **[[3oa5]], [[4dws]] – Chi – ''Yersinia entomophaga''<br />  | ||
| - | **[[3w4r]] –   | + | **[[3w4r]] – cbChi – corn borer<br />  | 
| + | **[[3wkz]] – cbChi (mutant)<br />  | ||
| + | **[[4mpi]] – HbChi chitin-binding domain – ''Hevea brasiliensis''<br />  | ||
| + | **[[4mst]] – HbChi catalytic domain <br />  | ||
*''Chitinase I binary complex''  | *''Chitinase I binary complex''  | ||
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**[[1hkk]], [[1hkm]], [[3rm4]], [[3rm8]], [[3rm9]], [[3rme]] – hChi catalytic domain  inhibitor<br />  | **[[1hkk]], [[1hkm]], [[3rm4]], [[3rm8]], [[3rm9]], [[3rme]] – hChi catalytic domain  inhibitor<br />  | ||
**[[1ll4]] - CiChi residues 36-427 + inhibitor<br />  | **[[1ll4]] - CiChi residues 36-427 + inhibitor<br />  | ||
| + | **[[3wl1]], [[3wqv]], [[3wqw]] – cbChi + GlcNAC<br />  | ||
| + | **[[3wl0]] – cbChi (mutant) + GlcNAC<br />  | ||
*Chitinase II  | *Chitinase II  | ||
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**[[2d49]] – SgChi chitin-binding domain - NMR<br />  | **[[2d49]] – SgChi chitin-binding domain - NMR<br />  | ||
**[[2xvp]] – AfChi<br />  | **[[2xvp]] – AfChi<br />  | ||
| - | **[[2xtk]] – AfChi + inhibitor  | + | **[[2xtk]], [[4tx6]] – AfChi + inhibitor<br />  | 
| + | **[[4toq]] – Chi - pomegrenate<br />  | ||
*Chitinase IV  | *Chitinase IV  | ||
**[[3hbd]], [[3hbe]], [[3hbh]] - Chi catalytic domain – Norway spruce<br />  | **[[3hbd]], [[3hbe]], [[3hbh]] - Chi catalytic domain – Norway spruce<br />  | ||
| + | **[[4mck]] – Chi - maize<br />  | ||
*Chitinase V  | *Chitinase V  | ||
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**[[3sim]] – Chi – ''Crocus vernus''  | **[[3sim]] – Chi – ''Crocus vernus''  | ||
| + | |||
| + | *Chitinase A  | ||
| + | |||
| + | **[[3wh1]], [[3wij]] – BcChiC + GlcNAC – ''Bryum coronatum''<br />  | ||
| + | **[[4ij4]] – BcChiC (mutant) + GlcNAC <br />  | ||
| + | **[[4mnj]] – spChi – sago palm<br />  | ||
| + | **[[4mnk]] – spChi + GlcNAC<br />  | ||
| + | **[[4mnl]], [[4mnm]] – spChi (mutant) + GlcNAC<br />  | ||
*Chitinase C  | *Chitinase C  | ||
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**[[3afb]] - PfChi catalytic domain (mutant)<br />   | **[[3afb]] - PfChi catalytic domain (mutant)<br />   | ||
**[[1cns]] – Chi – ''Hordeum vulgare''<br />  | **[[1cns]] – Chi – ''Hordeum vulgare''<br />  | ||
| - | **[[2czn]] - PfChi chitin-binding domain – NMR<br />  | + | **[[2czn]], [[2rts]] - PfChi chitin-binding domain – NMR<br />  | 
**[[2cwr]] - PfChi chitin-binding domain<br />  | **[[2cwr]] - PfChi chitin-binding domain<br />  | ||
**[[3ian]] – Chi (mutant) – ''Lactococcus lactis''<br />  | **[[3ian]] – Chi (mutant) – ''Lactococcus lactis''<br />  | ||
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**[[2uy2]] – yChi residues 22-315 – yeast<br />  | **[[2uy2]] – yChi residues 22-315 – yeast<br />  | ||
**[[4hmc]] – MmChi 60 – ''Moritella marina''<br />  | **[[4hmc]] – MmChi 60 – ''Moritella marina''<br />  | ||
| + | **[[4mb3]] – MmChi 60 (mutant)<br />  | ||
**[[3w3e]] – Chi – cowpea<br />  | **[[3w3e]] – Chi – cowpea<br />  | ||
**[[3w6b]] – RaChi catalytic domain – ''Ralstonia''<br />  | **[[3w6b]] – RaChi catalytic domain – ''Ralstonia''<br />  | ||
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**[[4hmd]] – MmChi 60 + intermediate<br />  | **[[4hmd]] – MmChi 60 + intermediate<br />  | ||
**[[4hme]] – MmChi 60 + NAG<br />  | **[[4hme]] – MmChi 60 + NAG<br />  | ||
| + | **[[4mb4]], [[4mb5]] – MmChi 60 (mutant) + NAG<br />  | ||
**[[3w6c]] – RaChi catalytic domain + disaccharide<br />  | **[[3w6c]] – RaChi catalytic domain + disaccharide<br />  | ||
**[[3w6d]], [[3w6f]] – RaChi catalytic domain (mutant) + polysaccharide<br />  | **[[3w6d]], [[3w6f]] – RaChi catalytic domain (mutant) + polysaccharide<br />  | ||
}}  | }}  | ||
[[Category:Topic Page]]  | [[Category:Topic Page]]  | ||
Revision as of 07:47, 16 March 2015
Chitinases cleave the beta-1-4-glycosidic bond between the N-acetyl-D-glucosamine units of which chitin is comprised. Chitinases are present in plants, bacteria and fungi. The first chitinase structures were solved in 1994, from a bacterium (1ctn) and a plant (2hvm). A mechanism for chitin cleavage was proposed based on several structures and was later confirmed.
3D Structures of Chitinase
Updated on 16-March-2015
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Marcin Jozef Suskiewicz, Anastassis Perrakis
