Chitinase

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spinqualitylabelsall models Chitinase A complex with (GlcNac)4 and ethylene glycol (PDB entry 3wh1) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Structural highlights 4 3D Structures of Chitinase Function 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. [1] Disease Chi is related to allergies and asthma. Structural highlights The of Chitinase A.[2] 3D Structures of Chitinase Chitinase 3D structures

3D Structures of Chitinase

Updated on 07-May-2019 {{#tree:id=OrganizedByTopic|openlevels=0|

• Chitinase I or chitotriosidase I

• • 5hbf – hChi - human
    
  • 4wjx, 4wka – hChi catalytic domain
    
  • 3aro, 3b8s – VhChi residues 22-597 – Vibrio harveyi
    
  • 3b9e - VhChi residues 22-597 (mutant)
    
  • 1k85 – BcChi fibronectin domain – Bacillus circulans – NMR
    
  • 1itx - BcChi catalytic domain
    
  • 1ed7 – BcChi chitin-binding domain - NMR
    
  • 1ll6, 1ll7 - CiChi residues 36-427 (mutant) – Coccicioides immitis
    
  • 1d2k - CiChi residues 36-427
    
  • 3n11 – BcChi – Bacillus cereus
    
  • 3iwr, 2dkv – Chi residues 33-340 – Japanese rice
    
  • 3g6l - BoChi residues 21-426 – Bionectria ochroleuca
    
  • 3oa5, 4dws, 4a5q – Chi – Yersinia entomophaga
    
  • 4mpi – HbChi chitin-binding domain – Hevea brasiliensis
    
  • 4mst – HbChi catalytic domain
    
  • 4tx7 – Chi – yard-long bean
    

• Chitinase I binary complex

• • 3arp, 3arq, 3arr, 3ars, 3art, 3aru, 3arv, 3arw, 3arx, 3ary, 3arz – VhChi residues 22-597 + inhibitor
    
  • 3as0, 3as1, 3as2, 3as3 – VhChi residues 22-597 (mutant) + inhibitor
    
  • 3b9a, 3b9d - VhChi residues 22-597 + polysaccharide
    
  • 2xvn, 2xuc – AfChi residues 29-307 + inhibitor – Aspergillus fumigatus
    
  • 3n13, 3n15, 3n17, 3n18 – BcChi (mutant) + NAG
    
  • 3n12 – BcChi + Zn
    
  • 3n1a - BcChi (mutant) + inhibitor
    
  • 3g6m - BoChi residues 21-426 + caffeine
    
  • 1waw, 1wb0, 4wk9, 4wkf, 4wkh – hChi catalytic domain + polypeptide – human
    
  • 1hkk, 1hkm, 3rm4, 3rm8, 3rm9, 3rme, 5nrf, 5nra, [[5nr8] – hChi catalytic domain + inhibitor
    
  • 1ll4 - CiChi residues 36-427 + inhibitor
    
  • 3wl1, 3wqv, 3wqw – cbChi + GlcNAC
    
  • 3wl0 – cbChi (mutant) + GlcNAC
    

• Chitinase II

• • 1e15, 3wd0 - SmChi
    
  • 1ogb, 1goi, 1e6p - SmChi (mutant)
    
  • 1kfw – Chi catalytic domain – Arthrobacter
    
  • 1dxj – Chi – Jack bean
    
  • 5y29 – OfChi catalytic domain 1 residues 1606-1992 – Ostrinia furnacalis
    
  • 5y2a – OfChi catalytic domain 2 residues 2056-2438
    

• Chitinase II binary complex

• • 1ogg, 1ur9 - SmChi (mutant) + inhibitor
    
  • 1e6n - SmChi (mutant) + polysaccharide
    
  • 1ur8, 1gpf, 1e6r, 3wd1, 3wd2, 3wd3, 3wd4 - SmChi + inhibitor
    
  • 1e6z – SmChi + intermediate
    
  • 2a3a, 2a3b, 2a3c, 2a3e – AfChi + inhibitor
    
  • 1w1p, 1w1t, 1w1v, 1w1y, 1o6i, 1h0g, 1h0i – SmChi + polypeptide
    
  • 5y2b – OfChi catalytic domain 1 + acetylchitooctaose
    
  • 5y2c – OfChi catalytic domain 2 (mutant) + acetylchitooctaose
    

• Chitinase III

• • 2dbt, 1wvu – SgChi residues 30-294 – Streptomyces griseus
    
  • 1wvv - SgChi residues 30-294 (mutant)
    
  • 2d49 – SgChi chitin-binding domain - NMR
    
  • 2xvp – AfChi
    
  • 2xtk, 4tx6 – AfChi + inhibitor
    
  • 4toq – Chi - pomegrenate
    
  • 5wup – OfChi residues 1-482
    
  • 5wv8 – OfChi residues 1-482 (mutant)
    
  • 5wv9 – OfChi residues 1-482 + GlcNAc
    
  • 5wvb – OfChi residues 1-482 (mutant) + GlcNAc
    
  • 5wus – OfChi residues 528-987
    
  • 5wvf – OfChi residues 528-987 (mutant)
    
  • 5wvh – OfChi residues 528-987 + GlcNAc
    
  • 5wvg – OfChi residues 528-987 (mutant) + GlcNAc
    

• Chitinase IV

• • 3hbd, 3hbe, 3hbh - Chi catalytic domain – Norway spruce
    
  • 4mck – Chi - maize
    
  • 5h7t – Chi chitinase domain – Japanese cedar
    

• Chitinase V

• • 3alf – tChi residues 26-377 – tobacco
    

• Chitinase V binary complex

• • 3alg - tChi residues 26-377 (mutant) + NAG
    
  • 3chc, 3chd, 3che, 3chf - AfChi + polypeptide
    
  • 3ch9, 2iuz – AfChi + inhibitor
    

• Chitinase VIII

• • 2cjl - Chi residues 41-244 – Streptomyces coelicolor
    

• Chitinase XVIII

• • 3sim – Chi – Crocus vernus

• Chitinase A

• • 3wh1, 3wij – BcChiA + GlcNAC – Bryum coronatum
    
  • 4ij4 – BcChiA (mutant) + GlcNAC
    
  • 4mnj, 4r5e – spChiA – sago palm
    
  • 4mnk – spChiA + GlcNAC
    
  • 4mnl, 4mnm – spChiA (mutant) + GlcNAC
    
  • 5dez – ApChiA + NAG – Autographa polyhedrosis
    
  • 5df0 – ApChiA + NAG + chitotriothiazoline
    
  • 5bum – ChiA LYSM domain – field horsetail
    
  • 1edq, 1ctn, 5zl9, 5z7o, 5z7n, 5z7m - SmChiA – Serratia marcescens
    
  • 1x6l, 1rd6 – SmChiA (mutant)
    
  • 1x6n - SmChi (mutant) + inhibitor
    
  • 1ffq, 2wk2, 2wly, 2wlz, 2wm0 - SmChi + inhibitor
    
  • 1nh6, 1k9t, 1ffr, 1eib, 1ehn - SmChi (mutant) + polysaccharide
    
  • 4pxv, 5ylg – PrChiA LYSM domain – Pteris ryukuensis
    
  • 4rl3 – PrChiA catalytic domain
    

• Chitinase B

• • 4z2g, 4z2h, 4z2i, 4z2j, 4z2k, 4z2l – SmChiB + inhibitor
    

• Chitinase C

• • 4dyg – RyChiC + NAG – Rye
    
  • 4dwx - RyChiC
    
  • 4j0l – RyChiC + GlcNAC
    
  • 4axn – SmChiC
    

• Chitinase H

• • 3w4r, 5gpr – cbChiH – corn borer
    
  • 3wkz – cbChiH (mutant)
    
  • 5gqb – cbChiH + chitohepatose
    

• Other chitinases

• • 1wno, 1w9p - AfChi
    
  • 2dsk - PfChi catalytic domain – Pyrococcus furiosus
    
  • 3afb - PfChi catalytic domain (mutant)
    
  • 1cns – Chi – Hordeum vulgare
    
  • 2czn, 2rts - PfChi chitin-binding domain – NMR
    
  • 2cwr - PfChi chitin-binding domain
    
  • 3ian – Chi (mutant) – Lactococcus lactis
    
  • 3fxy - hChi catalytic domain
    
  • 1lq0 - hChi residues 22-286
    
  • 1guv - hChi residues 22-387
    
  • 3fnd, 3co4 – Chi – Bacteroides thetaiotamicron
    
  • 3cql – Chi – Carica papaya
    
  • 2z37 - BjChi catalytic domain – Brassica juncea
    
  • 2z39 – BjChi catalytic domain (mutant)
    
  • 2uy2 – yChi residues 22-315 – yeast
    
  • 4hmc – MmChi 60 – Moritella marina
    
  • 4mb3 – MmChi 60 (mutant)
    
  • 3w3e – Chi – cowpea
    
  • 3w6b – RaChi catalytic domain – Ralstonia
    
  • 3w6e – RaChi catalytic domain (mutant)
    
  • 4w5z – Chi 60 catalytic domain – Vibrio marinus
    
  • 5kz6 – Chi – Bacillus anthracis
    
  • 5gzt, 5gzv, 5gzu – ChiW – Paeniacillus
    
  • 5dhd – TkChi CHBD2 domain – Thermococcus kodakarensis
    
  • 5dhe – TkChi CHBD3 domain
    
  • 5aa7 – Chi polusaccharide monooxygenase domain – Jonesia dentrificans
    
  • 4w5u – Chi 40 – Streptomyces thermoviolaceus
    
  • 4txg – Chi – Chromobacterium violaceum
    
  • 5vg0 – JdChi – Jonesia denitrificans
    
  • 5vg1 – JdChi – Neutron
    
  • 5k2l – Chi LYSM domain – Volvox carteri
    
  • 6idn – Chi – Ipomoea carnea
    
  • 6g9c, 6g9e – Chi – pig whipworm
    
  • 6bt9 – Chi – Bacillus thuringesis
    
  • 5yuq, 5xwq, 5xwf – Chi – Rhizomucor miehei
    

• Other chitinases binary complex

• • 3a4w, 3a4x – PfChi catalytic domain (mutant) + NAG
    
  • 1lg1 - hChi residues 22-387 + chitobiose
    
  • 1lg2 - hChi residues 22-387 + ethylene glycol
    
  • 3fy1, 2ybt, 2ybu - hChi catalytic domain + inhibitor
    
  • 1hki, 1hkj - hChi + inhibitor
    
  • 2z38 - BjChi catalytic domain + Cl
    
  • 2uy3, 2uy4, 2uy5 - yChi residues 22-315 + inhibitor
    
  • 1w9v, 1w9u - AfChi + polypeptide
    
  • 4hmd – MmChi 60 + intermediate
    
  • 4hme – MmChi 60 + NAG
    
  • 4mb4, 4mb5 – MmChi 60 (mutant) + NAG
    
  • 3w6c – RaChi catalytic domain + disaccharide
    
  • 3w6d, 3w6f – RaChi catalytic domain (mutant) + polysaccharide
    
  • 5xsv - TcChi residues 321-805 – Thermococcus chitonophagus
    
  • 5xsx, 5xsw - TcChi residues 321-805 + substrate
    

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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. ↑ 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