Template:STRUCTURE 1edq

File:1edq.png
Crystal Structure of Chitinase I from Serratia marcescens, 1edq


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. 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).






3D Structures of Chitinase3D Structures of Chitinase

Chitinase IChitinase I

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
1edq, 1ctn - SmChi – Serratia marcescens
1x6l, 1rd6 – SmChi (mutant)
3g6l - BoChi residues 21-426 – Bionectria ochroleuca

Chitinase I binary complexChitinase 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
1x6n - SmChi (mutant) + inhibitor
1ffq - SmChi + inhibitor
1nh6, 1k9t, 1ffr, 1eib, 1ehn - SmChi (mutant) + polysaccharide
2wk2, 2wly, 2wlz, 2wm0 – SmChi residues 2-520 + inhibitor
3g6m - BoChi residues 21-426 + caffeine
1waw, 1wb0 – hChi + polypeptide – human
1hkk, 1hkm – hChi + inhibitor
1ll4 - CiChi residues 36-427 + inhibitor

Chitinase IIChitinase II

1e15 - SmChi 1ogb, 1goi, 1e6p - SmChi (mutant) 1kfw – Chi catalytic domain – Arthrobacter 1dxj – Chi – Jack bean

Chitinase II binary complexChitinase II binary complex

1ogg, 1ur9 - SmChi (mutant) + inhibitor 1e6n - SmChi (mutant) + polysaccharide 1ur8, 1gpf, 1e6r - SmChi + inhibitor 1e6z – SmChi + intermediate 2a3a, 2a3b, 2a3c, 2a3e – AfChi + inhibitor 1w1p, 1w1t, 1w1v, 1w1y, 1o6i, 1h0g, 1h0i – SmChi + polypeptide

Chitinase IIIChitinase III

2dbt, 2wvu – SgChi residues 30-294 – Streptomyces griseus 1wvv - SgChi residues 30-294 (mutant) 2d49 – SgChi chitin-binding domain - NMR

Chitinase IVChitinase IV

3hbd, 3hbe, 3hbh - Chi catalytic domain – Norway spruce

Chitinase VChitinase V

3alf – tChi residues 26-377 – tobacco

Chitinase V binary complexChitinase V binary complex

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

Chitinase VIIIChitinase VIII

2cjl - Chi residues 41-244 – Streptomyces coelicolor

ChitinaseChitinase

1wno, 1w9p - AfChi 2dsk - PfChi catalytic domain – Pyrococcus furiosus 3afb - PfChi catalytic domain (mutant) 1cns – Chi – Hordeum vulgare 2czn - 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

Chitinase binary complexChitinase binary complex

3a4w, 3a4x – PfChi catalytic domain (mutant) + NAG 1lg1 - hChi residues 22-387 + chitobiose 1lg2 - hChi residues 22-387 + ethylene glycol 3fy1 - 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Anastassis Perrakis, Alexander Berchansky, Michal Harel, Marcin Jozef Suskiewicz