Chitinase

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[[Image:1edq.png|left|200px|thumb|Crystal Structure of Chitinase I from ''Serratia marcescens'', [[1edq]]]]
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<StructureSection load='3wh1' size='350' side='right' caption='Chitinase A complex with (GlcNac)4 and ethylene glycol (PDB entry [[3wh1]])' scene='27/271631/Cv/3'>
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{{STRUCTURE_1edq| PDB=1edq | SIZE=400| SCENE=Chitinases/Cv/2 |right|CAPTION=Chitinase I from ''Serratia marcescens'', [[1edq]] }}
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__TOC__
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== Function ==
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[[Chitinase]]s (Chi) 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. <ref>PMID:21054166</ref>. <br />
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* '''Chitinase I''' is found in plants.<br />
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* '''Chitinase II''' is found in plants, fungi and bacteria.<br />
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* '''Chitinase III''' has no sequence similarity to class I or II.<br />
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* '''Chitinase IV''' has similar characteristics to class I but are smaller than it.<br />
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==Disease ==
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Chi is related to allergies and asthma<ref>PMID:19295241</ref>.
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== Structural highlights ==
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The <scene name='27/271631/Cv/5'>chitin tetrasaccharide binding site</scene> of Chitinase A. <ref>PMID:24582745</ref> Water molecules are shown as red spheres.
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[[Chitinase]]s 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. The images at the left and at the right correspond to one representative Chitinase, ''i.e.'' the crystal structure of Chitinase I from ''Serratia marcescens'' ([[1edq]]).
 
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== 3D Structures of Chitinase ==
== 3D Structures of Chitinase ==
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[[Chitinase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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===Chitinase I===
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[[3aro]], [[3b8s]] – VhChi residues 22-597 – ''Vibrio harveyi''<br />
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[[3b9e]] - VhChi residues 22-597 (mutant)<br />
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[[1k85]] – BcChi fibronectin domain – ''Bacillus circulans'' – NMR<br />
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[[1itx]] - BcChi catalytic domain<br />
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[[1ed7]] – BcChi chitin-binding domain - NMR<br />
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[[1ll6]], [[1ll7]] - CiChi residues 36-427 (mutant) – ''Coccicioides immitis'' <br />
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[[1d2k]] - CiChi residues 36-427<br />
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[[3n11]] – BcChi – ''Bacillus cereus''<br />
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[[3iwr]], [[2dkv]] – Chi residues 33-340 – Japanese rice<br />
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[[1edq]], [[1ctn]], [[4axn]] - SmChi – ''Serratia marcescens''<br />
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[[1x6l]], [[1rd6]] – SmChi (mutant)<br />
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[[3g6l]] - BoChi residues 21-426 – ''Bionectria ochroleuca''<br />
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[[3oa5]], [[4dws]] – Chi – ''Yersinia entomophaga''<br />
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[[3w4r]] – Chi – corn borer<br />
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====Chitinase I binary complex====
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[[3arp]], [[3arq]], [[3arr]], [[3ars]], [[3art]], [[3aru]], [[3arv]], [[3arw]], [[3arx]], [[3ary]], [[3arz]] – VhChi residues 22-597 + inhibitor<br />
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[[3as0]], [[3as1]], [[3as2]], [[3as3]] – VhChi residues 22-597 (mutant) + inhibitor<br />
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[[3b9a]], [[3b9d]] - VhChi residues 22-597 + polysaccharide<br />
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[[2xvn]], [[2xuc]] – AfChi residues 29-307 + inhibitor – ''Aspergillus fumigatus''<br />
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[[3n13]], [[3n15]], [[3n17]], [[3n18]] – BcChi (mutant) + NAG<br />
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[[3n12]] – BcChi + Zn<br />
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[[3n1a]] - BcChi (mutant) + inhibitor<br />
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[[1x6n]] - SmChi (mutant) + inhibitor<br />
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[[1ffq]] - SmChi + inhibitor<br />
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[[1nh6]], [[1k9t]], [[1ffr]], [[1eib]], [[1ehn]] - SmChi (mutant) + polysaccharide<br />
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[[2wk2]], [[2wly]], [[2wlz]], [[2wm0]] – SmChi residues 2-520 + inhibitor <br />
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[[3g6m]] - BoChi residues 21-426 + caffeine<br />
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[[1waw]], [[1wb0]] – hChi catalytic domain polypeptide – human<br />
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[[1hkk]], [[1hkm]], [[3rm4]], [[3rm8]], [[3rm9]], [[3rme]] – hChi catalytic domain inhibitor<br />
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[[1ll4]] - CiChi residues 36-427 + inhibitor<br />
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===Chitinase II===
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[[1e15]], [[3wd0]] - SmChi<br />
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[[1ogb]], [[1goi]], [[1e6p]] - SmChi (mutant)<br />
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[[1kfw]] – Chi catalytic domain – Arthrobacter<br />
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[[1dxj]] – Chi – Jack bean<br />
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====Chitinase II binary complex====
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[[1ogg]], [[1ur9]] - SmChi (mutant) + inhibitor<br />
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[[1e6n]] - SmChi (mutant) + polysaccharide<br />
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[[1ur8]], [[1gpf]], [[1e6r]], [[3wd1]], [[3wd2]], [[3wd3]], [[3wd4]] - SmChi + inhibitor<br />
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[[1e6z]] – SmChi + intermediate<br />
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[[2a3a]], [[2a3b]], [[2a3c]], [[2a3e]] – AfChi + inhibitor<br />
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[[1w1p]], [[1w1t]], [[1w1v]], [[1w1y]], [[1o6i]], [[1h0g]], [[1h0i]] – SmChi + polypeptide<br />
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===Chitinase III===
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[[2dbt]], [[1wvu]] – SgChi residues 30-294 – ''Streptomyces griseus''<br />
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[[1wvv]] - SgChi residues 30-294 (mutant)<br />
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[[2d49]] – SgChi chitin-binding domain - NMR<br />
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[[2xvp]] – AfChi<br />
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[[2xtk]] – AfChi + inhibitor
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===Chitinase IV===
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[[3hbd]], [[3hbe]], [[3hbh]] - Chi catalytic domain – Norway spruce<br />
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===Chitinase V===
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[[3alf]] – tChi residues 26-377 – tobacco<br />
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====Chitinase V binary complex====
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[[3alg]] - tChi residues 26-377 (mutant) + NAG<br />
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[[3chc]], [[3chd]], [[3che]], [[3chf]] - AfChi + polypeptide<br />
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[[3ch9]], [[2iuz]] – AfChi + inhibitor<br />
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===Chitinase VIII===
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[[2cjl]] - Chi residues 41-244 – ''Streptomyces coelicolor''<br />
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===Chitinase XVIII===
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[[3sim]] – Chi – ''Crocus vernus''
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===Chitinase C===
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[[4dyg]] – RyChiC + NAG – Rye<br />
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[[4dwx]] - RyChiC<br />
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[[4j0l]] – RyChiC + GlcNAC<br />
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===Chitinase===
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[[1wno]], [[1w9p]] - AfChi<br />
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[[2dsk]] - PfChi catalytic domain – ''Pyrococcus furiosus''<br />
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[[3afb]] - PfChi catalytic domain (mutant)<br />
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[[1cns]] – Chi – ''Hordeum vulgare''<br />
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[[2czn]] - PfChi chitin-binding domain – NMR<br />
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[[2cwr]] - PfChi chitin-binding domain<br />
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[[3ian]] – Chi (mutant) – ''Lactococcus lactis''<br />
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[[3fxy]] - hChi catalytic domain<br />
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[[1lq0]] - hChi residues 22-286<br />
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[[1guv]] - hChi residues 22-387<br />
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[[3fnd]], [[3co4]] – Chi – ''Bacteroides thetaiotamicron''<br />
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[[3cql]] – Chi – ''Carica papaya''<br />
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[[2z37]] - BjChi catalytic domain – ''Brassica juncea''<br />
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[[2z39]] – BjChi catalytic domain (mutant)<br />
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[[2uy2]] – yChi residues 22-315 – yeast<br />
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[[4hmc]] – MmChi 60 – ''Moritella marina''<br />
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[[3w3e]] – Chi – cowpea<br />
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[[3w6b]] – RaChi catalytic domain – ''Ralstonia''<br />
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[[3w6e]] – RaChi catalytic domain (mutant) <br />
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====Chitinase binary complex====
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[[3a4w]], [[3a4x]] – PfChi catalytic domain (mutant) + NAG<br />
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[[1lg1]] - hChi residues 22-387 + chitobiose<br />
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[[1lg2]] - hChi residues 22-387 + ethylene glycol<br />
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[[3fy1]], [[2ybt]], [[2ybu]] - hChi catalytic domain + inhibitor<br />
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[[1hki]], [[1hkj]] - hChi + inhibitor<br />
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[[2z38]] - BjChi catalytic domain + Cl<br />
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[[2uy3]], [[2uy4]], [[2uy5]] - yChi residues 22-315 + inhibitor<br />
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[[1w9v]], [[1w9u]] - AfChi + polypeptide<br />
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[[4hmd]] – MmChi 60 + intermediate<br />
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[[4hme]] – MmChi 60 + NAG<br />
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[[3w6c]] – RaChi catalytic domain + disaccharide<br />
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[[3w6d]], [[3w6f]] – RaChi catalytic domain (mutant) + polysaccharide<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Chitinase A complex with (GlcNac)4 and ethylene glycol (PDB entry 3wh1)

Drag the structure with the mouse to rotate

References

  1. ↑ Lee CG, Da Silva CA, Dela Cruz CS, Ahangari F, Ma B, Kang MJ, He CH, Takyar S, Elias JA. Role of chitin and chitinase/chitinase-like proteins in inflammation, tissue remodeling, and injury. Annu Rev Physiol. 2011;73:479-501. doi: 10.1146/annurev-physiol-012110-142250. PMID:21054166 doi:http://dx.doi.org/10.1146/annurev-physiol-012110-142250
  2. ↑ Shuhui L, Mok YK, Wong WS. Role of mammalian chitinases in asthma. Int Arch Allergy Immunol. 2009;149(4):369-77. doi: 10.1159/000205583. Epub 2009, Mar 17. PMID:19295241 doi:http://dx.doi.org/10.1159/000205583
  3. ↑ Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T. Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center. Biochim Biophys Acta. 2014 Feb 25;1844(4):793-802. doi:, 10.1016/j.bbapap.2014.02.013. PMID:24582745 doi:http://dx.doi.org/10.1016/j.bbapap.2014.02.013
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