Chitinase
From Proteopedia
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== Function == | == Function == | ||
- | [[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. <ref>PMID:21054166</ref> | + | [[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 /> |
+ | * '''Chitinase I''' is found in plants.<br /> | ||
+ | * '''Chitinase II''' is found in plants, fungi and bacteria.<br /> | ||
+ | * '''Chitinase III''' has no sequence similarity to class I or II.<br /> | ||
+ | * '''Chitinase IV''' has similar characteristics to class I but are smaller than it.<br /> | ||
==Disease == | ==Disease == | ||
- | Chi is related to allergies and asthma. | + | Chi is related to allergies and asthma<ref>PMID:19295241</ref>. |
== Structural highlights == | == Structural highlights == | ||
- | The <scene name='27/271631/Cv/5'>chitin tetrasaccharide binding site</scene> of Chitinase A.<ref>PMID:24582745</ref> | + | 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. |
== 3D Structures of Chitinase == | == 3D Structures of Chitinase == | ||
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</StructureSection> | </StructureSection> | ||
- | == 3D Structures of Chitinase == | ||
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- | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
- | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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- | *Chitinase I or chitotriosidase I | ||
- | |||
- | **[[5hbf]] – hChi - human<br /> | ||
- | **[[4wjx]], [[4wka]] – hChi catalytic domain<br /> | ||
- | **[[3aro]], [[3b8s]] – VhChi residues 22-597 – ''Vibrio harveyi''<br /> | ||
- | **[[3b9e]] - VhChi residues 22-597 (mutant)<br /> | ||
- | **[[1k85]] – BcChi fibronectin domain – ''Bacillus circulans'' – NMR<br /> | ||
- | **[[1itx]] - BcChi catalytic domain<br /> | ||
- | **[[1ed7]] – BcChi chitin-binding domain - NMR<br /> | ||
- | **[[1ll6]], [[1ll7]] - CiChi residues 36-427 (mutant) – ''Coccicioides immitis'' <br /> | ||
- | **[[1d2k]] - CiChi residues 36-427<br /> | ||
- | **[[3n11]] – BcChi – ''Bacillus cereus''<br /> | ||
- | **[[3iwr]], [[2dkv]] – Chi residues 33-340 – Japanese rice<br /> | ||
- | **[[3g6l]] - BoChi residues 21-426 – ''Bionectria ochroleuca''<br /> | ||
- | **[[3oa5]], [[4dws]], [[4a5q]] – Chi – ''Yersinia entomophaga''<br /> | ||
- | **[[4mpi]] – HbChi chitin-binding domain – ''Hevea brasiliensis''<br /> | ||
- | **[[4mst]] – HbChi catalytic domain <br /> | ||
- | **[[4tx7]] – Chi – yard-long bean<br /> | ||
- | |||
- | *''Chitinase I binary complex'' | ||
- | |||
- | **[[3arp]], [[3arq]], [[3arr]], [[3ars]], [[3art]], [[3aru]], [[3arv]], [[3arw]], [[3arx]], [[3ary]], [[3arz]] – VhChi residues 22-597 + inhibitor<br /> | ||
- | **[[3as0]], [[3as1]], [[3as2]], [[3as3]] – VhChi residues 22-597 (mutant) + inhibitor<br /> | ||
- | **[[3b9a]], [[3b9d]] - VhChi residues 22-597 + polysaccharide<br /> | ||
- | **[[2xvn]], [[2xuc]] – AfChi residues 29-307 + inhibitor – ''Aspergillus fumigatus''<br /> | ||
- | **[[3n13]], [[3n15]], [[3n17]], [[3n18]] – BcChi (mutant) + NAG<br /> | ||
- | **[[3n12]] – BcChi + Zn<br /> | ||
- | **[[3n1a]] - BcChi (mutant) + inhibitor<br /> | ||
- | **[[3g6m]] - BoChi residues 21-426 + caffeine<br /> | ||
- | **[[1waw]], [[1wb0]], [[4wk9]], [[4wkf]], [[4wkh]] – hChi catalytic domain + polypeptide – human<br /> | ||
- | **[[1hkk]], [[1hkm]], [[3rm4]], [[3rm8]], [[3rm9]], [[3rme]], [[5nrf]], [[5nra]], [[5nr8] – hChi catalytic domain + inhibitor<br /> | ||
- | **[[1ll4]] - CiChi residues 36-427 + inhibitor<br /> | ||
- | **[[3wl1]], [[3wqv]], [[3wqw]] – cbChi + GlcNAC<br /> | ||
- | **[[3wl0]] – cbChi (mutant) + GlcNAC<br /> | ||
- | |||
- | *Chitinase II | ||
- | |||
- | **[[1e15]], [[3wd0]] - SmChi<br /> | ||
- | **[[1ogb]], [[1goi]], [[1e6p]] - SmChi (mutant)<br /> | ||
- | **[[1kfw]] – Chi catalytic domain – Arthrobacter<br /> | ||
- | **[[1dxj]] – Chi – Jack bean<br /> | ||
- | **[[5y29]] – OfChi catalytic domain 1 residues 1606-1992 – ''Ostrinia furnacalis''<br /> | ||
- | **[[5y2a]] – OfChi catalytic domain 2 residues 2056-2438<br /> | ||
- | |||
- | *''Chitinase II binary complex'' | ||
- | |||
- | **[[1ogg]], [[1ur9]] - SmChi (mutant) + inhibitor<br /> | ||
- | **[[1e6n]] - SmChi (mutant) + polysaccharide<br /> | ||
- | **[[1ur8]], [[1gpf]], [[1e6r]], [[3wd1]], [[3wd2]], [[3wd3]], [[3wd4]] - SmChi + inhibitor<br /> | ||
- | **[[1e6z]] – SmChi + intermediate<br /> | ||
- | **[[2a3a]], [[2a3b]], [[2a3c]], [[2a3e]] – AfChi + inhibitor<br /> | ||
- | **[[1w1p]], [[1w1t]], [[1w1v]], [[1w1y]], [[1o6i]], [[1h0g]], [[1h0i]] – SmChi + polypeptide<br /> | ||
- | **[[5y2b]] – OfChi catalytic domain 1 + acetylchitooctaose<br /> | ||
- | **[[5y2c]] – OfChi catalytic domain 2 (mutant) + acetylchitooctaose<br /> | ||
- | |||
- | *Chitinase III | ||
- | |||
- | **[[2dbt]], [[1wvu]] – SgChi residues 30-294 – ''Streptomyces griseus''<br /> | ||
- | **[[1wvv]] - SgChi residues 30-294 (mutant)<br /> | ||
- | **[[2d49]] – SgChi chitin-binding domain - NMR<br /> | ||
- | **[[2xvp]] – AfChi<br /> | ||
- | **[[2xtk]], [[4tx6]] – AfChi + inhibitor<br /> | ||
- | **[[4toq]] – Chi - pomegrenate<br /> | ||
- | **[[5wup]] – OfChi residues 1-482<br /> | ||
- | **[[5wv8]] – OfChi residues 1-482 (mutant)<br /> | ||
- | **[[5wv9]] – OfChi residues 1-482 + GlcNAc<br /> | ||
- | **[[5wvb]] – OfChi residues 1-482 (mutant) + GlcNAc<br /> | ||
- | **[[5wus]] – OfChi residues 528-987<br /> | ||
- | **[[5wvf]] – OfChi residues 528-987 (mutant)<br /> | ||
- | **[[5wvh]] – OfChi residues 528-987 + GlcNAc<br /> | ||
- | **[[5wvg]] – OfChi residues 528-987 (mutant) + GlcNAc<br /> | ||
- | |||
- | *Chitinase IV | ||
- | |||
- | **[[3hbd]], [[3hbe]], [[3hbh]] - Chi catalytic domain – Norway spruce<br /> | ||
- | **[[4mck]] – Chi - maize<br /> | ||
- | **[[5h7t]] – Chi chitinase domain – Japanese cedar<br /> | ||
- | |||
- | *Chitinase V | ||
- | |||
- | **[[3alf]] – tChi residues 26-377 – tobacco<br /> | ||
- | |||
- | *''Chitinase V binary complex'' | ||
- | |||
- | **[[3alg]] - tChi residues 26-377 (mutant) + NAG<br /> | ||
- | **[[3chc]], [[3chd]], [[3che]], [[3chf]] - AfChi + polypeptide<br /> | ||
- | **[[3ch9]], [[2iuz]] – AfChi + inhibitor<br /> | ||
- | |||
- | *Chitinase VIII | ||
- | |||
- | **[[2cjl]] - Chi residues 41-244 – ''Streptomyces coelicolor''<br /> | ||
- | |||
- | *Chitinase XVIII | ||
- | |||
- | **[[3sim]] – Chi – ''Crocus vernus'' | ||
- | |||
- | *Chitinase A | ||
- | |||
- | **[[3wh1]], [[3wij]] – BcChiA + GlcNAC – ''Bryum coronatum''<br /> | ||
- | **[[4ij4]] – BcChiA (mutant) + GlcNAC <br /> | ||
- | **[[4mnj]], [[4r5e]] – spChiA – sago palm<br /> | ||
- | **[[4mnk]] – spChiA + GlcNAC<br /> | ||
- | **[[4mnl]], [[4mnm]] – spChiA (mutant) + GlcNAC<br /> | ||
- | **[[5dez]] – ApChiA + NAG – ''Autographa polyhedrosis''<br /> | ||
- | **[[5df0]] – ApChiA + NAG + chitotriothiazoline<br /> | ||
- | **[[5bum]] – ChiA LYSM domain – field horsetail<br /> | ||
- | **[[1edq]], [[1ctn]], [[5zl9]], [[5z7o]], [[5z7n]], [[5z7m]] - SmChiA – ''Serratia marcescens''<br /> | ||
- | **[[1x6l]], [[1rd6]] – SmChiA (mutant)<br /> | ||
- | **[[1x6n]] - SmChi (mutant) + inhibitor<br /> | ||
- | **[[1ffq]], [[2wk2]], [[2wly]], [[2wlz]], [[2wm0]] - SmChi + inhibitor<br /> | ||
- | **[[1nh6]], [[1k9t]], [[1ffr]], [[1eib]], [[1ehn]] - SmChi (mutant) + polysaccharide<br /> | ||
- | **[[4pxv]], [[5ylg]] – PrChiA LYSM domain – ''Pteris ryukuensis''<br /> | ||
- | **[[4rl3]] – PrChiA catalytic domain <br /> | ||
- | |||
- | *Chitinase B | ||
- | |||
- | **[[4z2g]], [[4z2h]], [[4z2i]], [[4z2j]], [[4z2k]], [[4z2l]] – SmChiB + inhibitor<br /> | ||
- | |||
- | *Chitinase C | ||
- | |||
- | **[[4dyg]] – RyChiC + NAG – Rye<br /> | ||
- | **[[4dwx]] - RyChiC<br /> | ||
- | **[[4j0l]] – RyChiC + GlcNAC<br /> | ||
- | **[[4axn]] – SmChiC<br /> | ||
- | |||
- | * Chitinase H | ||
- | |||
- | **[[3w4r]], [[5gpr]] – cbChiH – corn borer<br /> | ||
- | **[[3wkz]] – cbChiH (mutant)<br /> | ||
- | **[[5gqb]] – cbChiH + chitohepatose<br /> | ||
- | |||
- | *Other chitinases | ||
- | |||
- | **[[1wno]], [[1w9p]] - AfChi<br /> | ||
- | **[[2dsk]] - PfChi catalytic domain – ''Pyrococcus furiosus''<br /> | ||
- | **[[3afb]] - PfChi catalytic domain (mutant)<br /> | ||
- | **[[1cns]] – Chi – ''Hordeum vulgare''<br /> | ||
- | **[[2czn]], [[2rts]] - PfChi chitin-binding domain – NMR<br /> | ||
- | **[[2cwr]] - PfChi chitin-binding domain<br /> | ||
- | **[[3ian]] – Chi (mutant) – ''Lactococcus lactis''<br /> | ||
- | **[[3fxy]] - hChi catalytic domain<br /> | ||
- | **[[1lq0]] - hChi residues 22-286<br /> | ||
- | **[[1guv]] - hChi residues 22-387<br /> | ||
- | **[[3fnd]], [[3co4]] – Chi – ''Bacteroides thetaiotamicron''<br /> | ||
- | **[[3cql]] – Chi – ''Carica papaya''<br /> | ||
- | **[[2z37]] - BjChi catalytic domain – ''Brassica juncea''<br /> | ||
- | **[[2z39]] – BjChi catalytic domain (mutant)<br /> | ||
- | **[[2uy2]] – yChi residues 22-315 – yeast<br /> | ||
- | **[[4hmc]] – MmChi 60 – ''Moritella marina''<br /> | ||
- | **[[4mb3]] – MmChi 60 (mutant)<br /> | ||
- | **[[3w3e]] – Chi – cowpea<br /> | ||
- | **[[3w6b]] – RaChi catalytic domain – ''Ralstonia''<br /> | ||
- | **[[3w6e]] – RaChi catalytic domain (mutant) <br /> | ||
- | **[[4w5z]] – Chi 60 catalytic domain – ''Vibrio marinus''<br /> | ||
- | **[[5kz6]] – Chi – ''Bacillus anthracis''<br /> | ||
- | **[[5gzt]], [[5gzv]], [[5gzu]] – ChiW – ''Paeniacillus'' <br /> | ||
- | **[[5dhd]] – TkChi CHBD2 domain – ''Thermococcus kodakarensis''<br /> | ||
- | **[[5dhe]] – TkChi CHBD3 domain <br /> | ||
- | **[[5aa7]] – Chi polusaccharide monooxygenase domain – ''Jonesia dentrificans''<br /> | ||
- | **[[4w5u]] – Chi 40 – ''Streptomyces thermoviolaceus''<br /> | ||
- | **[[4txg]] – Chi – ''Chromobacterium violaceum''<br /> | ||
- | **[[5vg0]] – JdChi – ''Jonesia denitrificans''<br /> | ||
- | **[[5vg1]] – JdChi – Neutron<br /> | ||
- | **[[5k2l]] – Chi LYSM domain – ''Volvox carteri''<br /> | ||
- | **[[6idn]] – Chi – ''Ipomoea carnea''<br /> | ||
- | **[[6g9c]], [[6g9e]] – Chi – pig whipworm<br /> | ||
- | **[[6bt9]] – Chi – ''Bacillus thuringesis''<br /> | ||
- | **[[5yuq]], [[5xwq]], [[5xwf]] – Chi – ''Rhizomucor miehei''<br /> | ||
- | |||
- | *''Other chitinases binary complex'' | ||
- | **[[3a4w]], [[3a4x]] – PfChi catalytic domain (mutant) + NAG<br /> | ||
- | **[[1lg1]] - hChi residues 22-387 + chitobiose<br /> | ||
- | **[[1lg2]] - hChi residues 22-387 + ethylene glycol<br /> | ||
- | **[[3fy1]], [[2ybt]], [[2ybu]] - hChi catalytic domain + inhibitor<br /> | ||
- | **[[1hki]], [[1hkj]] - hChi + inhibitor<br /> | ||
- | **[[2z38]] - BjChi catalytic domain + Cl<br /> | ||
- | **[[2uy3]], [[2uy4]], [[2uy5]] - yChi residues 22-315 + inhibitor<br /> | ||
- | **[[1w9v]], [[1w9u]] - AfChi + polypeptide<br /> | ||
- | **[[4hmd]] – MmChi 60 + intermediate<br /> | ||
- | **[[4hme]] – MmChi 60 + NAG<br /> | ||
- | **[[4mb4]], [[4mb5]] – MmChi 60 (mutant) + NAG<br /> | ||
- | **[[3w6c]] – RaChi catalytic domain + disaccharide<br /> | ||
- | **[[3w6d]], [[3w6f]] – RaChi catalytic domain (mutant) + polysaccharide<br /> | ||
- | **[[5xsv]] - TcChi residues 321-805 – ''Thermococcus chitonophagus''<br /> | ||
- | **[[5xsx]], [[5xsw]] - TcChi residues 321-805 + substrate <br /> | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
|
References
- ↑ 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
- ↑ 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
- ↑ 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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