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InterPro: IPR002196 Glycoside hydrolase, family 24

Protein matchesHelp
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UniProtKB
Matches:
1068 proteins
AccessionHelp
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IPR002196 Glyco_hydro_24
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Family
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InterPro RelationshipsHelp
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Children IPR001165 Glycoside hydrolase, family 24, T4 lysozyme
GO Term annotationHelp
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Process GO:0009253 peptidoglycan catabolic process
GO:0016998 cell wall macromolecule catabolic process
Function GO:0003796 lysozyme activity
InterPro annotation
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AbstractHelp
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O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.

Glycoside hydrolase family 24 GH24 comprises enzymes with only one known activity; lysozyme (EC:3.2.1.17).

This entry includes Bacteriophage lambda lysozyme and Escherichia coli endolysin [5]. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of prokaryotic cell walls. E. coli endolysin also functions in bacterial cell lysis and acts as a transglycosylase. The Bacteriophage T4 lysozyme structure contains 2 domains, the interface between which forms the active-site cleft. The N terminus of the 2 domains undergoes a 'hinge-bending' motion about an axis passing through the molecular waist [5, 6]. This mobility is thought to be important in allowing access of substrates to the enzyme active site.
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102l , 103l , 104l , 107l , 108l , 109l , 110l , 111l , 112l , 113l , 114l , 115l , 118l , 119l , 120l , 122l , 123l , 125l , 126l , 127l , 128l , 129l , 130l , 131l , 137l , 138l , 139l , 140l , 141l , 142l , 143l , 144l , 145l , 146l , 147l , 148l , 149l , 150l , 151l , 152l , 155l , 156l , 157l , 158l , 159l , 160l , 161l , 162l , 163l , 164l , 165l , 166l , 167l , 168l , 169l , 170l , 171l , 172l , 173l , 174l , 175l , 176l , 177l , 178l , 180l , 181l , 182l , 183l , 184l , 185l , 186l , 187l , 188l , 189l , 190l , 191l , 192l , 195l , 196l , 197l , 198l , 199l , 1am7 , 1b6i , 1c60 , 1c61 , 1c62 , 1c63 , 1c64 , 1c65 , 1c66 , 1c67 , 1c68 , 1c69 , 1c6a , 1c6b , 1c6c , 1c6d , 1c6e , 1c6f , 1c6g , 1c6h , 1c6i , 1c6j , 1c6k , 1c6l , 1c6m , 1c6n , 1c6p , 1c6q , 1c6t , 1ctw , 1cu0 , 1cu2 , 1cu3 , 1cu5 , 1cu6 , 1cup , 1cuq , 1cv0 , 1cv1 , 1cv3 , 1cv4 , 1cv5 , 1cv6 , 1cvk , 1cx6 , 1cx7 , 1d2w , 1d2y , 1d3f , 1d3j , 1d3m , 1d3n , 1d9u , 1d9w , 1dya , 1dyb , 1dyc , 1dyd , 1dye , 1dyf , 1dyg , 1epy , 1g06 , 1g07 , 1g0g , 1g0j , 1g0k , 1g0l , 1g0m , 1g0p , 1g0q , 1g1v , 1g1w , 1i6s , 1jqu , 1jtm , 1jtn , 1k28 , 1kni , 1ks3 , 1kw5 , 1kw7 , 1ky0 , 1ky1 , 1l00 , 1l01 , 1l02 , 1l03 , 1l04 , 1l05 , 1l06 , 1l07 , 1l08 , 1l09 , 1l0j , 1l0k , 1l10 , 1l11 , 1l12 , 1l13 , 1l14 , 1l15 , 1l16 , 1l17 , 1l18 , 1l19 , 1l20 , 1l21 , 1l22 , 1l23 , 1l24 , 1l25 , 1l26 , 1l27 , 1l28 , 1l29 , 1l30 , 1l31 , 1l32 , 1l33 , 1l34 , 1l35 , 1l36 , 1l37 , 1l38 , 1l39 , 1l40 , 1l41 , 1l42 , 1l43 , 1l44 , 1l45 , 1l46 , 1l47 , 1l48 , 1l49 , 1l50 , 1l51 , 1l52 , 1l53 , 1l54 , 1l55 , 1l56 , 1l57 , 1l58 , 1l59 , 1l60 , 1l61 , 1l62 , 1l63 , 1l64 , 1l65 , 1l66 , 1l67 , 1l68 , 1l69 , 1l70 , 1l71 , 1l72 , 1l73 , 1l74 , 1l75 , 1l76 , 1l77 , 1l79 , 1l80 , 1l81 , 1l82 , 1l83 , 1l84 , 1l85 , 1l86 , 1l87 , 1l88 , 1l89 , 1l90 , 1l91 , 1l92 , 1l93 , 1l94 , 1l95 , 1l96 , 1l97 , 1l98 , 1l99 , 1lgu , 1lgw , 1lgx , 1li2 , 1li3 , 1li6 , 1llh , 1lpy , 1lw9 , 1lwg , 1lwk , 1lyd , 1lye , 1lyf , 1lyg , 1lyh , 1lyi , 1lyj , 1nhb , 1ov5 , 1ov7 , 1ovh , 1ovj , 1ovk , 1owy , 1owz , 1oyu , 1p2l , 1p2r , 1p36 , 1p37 , 1p3n , 1p46 , 1p56 , 1p5c , 1p64 , 1p6y , 1p7s , 1pqd , 1pqi , 1pqj , 1pqk , 1pqm , 1pqo , 1qs5 , 1qs9 , 1qsb , 1qsq , 1qt3 , 1qt4 , 1qt5 , 1qt6 , 1qt7 , 1qt8 , 1qtb , 1qtc , 1qtd , 1qth , 1qtv , 1qtz , 1qud , 1qug , 1quh , 1quo , 1ssw , 1ssy , 1swy , 1swz , 1sx2 , 1sx7 , 1t6h , 1t8a , 1t8f , 1t8g , 1t97 , 1tla , 1xep , 1xjt , 1xju , 1zur , 1zwn , 1zyt , 200l , 201l , 205l , 206l , 209l , 210l , 211l , 212l , 213l , 214l , 215l , 216l , 217l , 218l , 219l , 220l , 221l , 222l , 223l , 224l , 225l , 226l , 227l , 228l , 229l , 230l , 231l , 232l , 233l , 234l , 235l , 236l , 237l , 238l , 239l , 240l , 241l , 242l , 243l , 244l , 245l , 246l , 247l , 248l , 249l , 250l , 251l , 252l , 253l , 254l , 255l , 256l , 257l , 258l , 259l , 260l , 261l , 262l , 2a4t , 2b6t , 2b6w , 2b6x , 2b6y , 2b6z , 2b70 , 2b72 , 2b73 , 2b74 , 2b75 , 2b7w , 2b7x , 2cuu , 2f2q , 2f32 , 2f47 , 2huk , 2hul , 2hum , 2igc , 2l78 , 2lzm , 2ntg , 2nth , 2o79 , 2oe4 , 2oe7 , 2oe9 , 2oea , 2oty , 2otz , 2ou0 , 2ou8 , 2ou9 , 2q9d , 2q9e , 2qar , 2ray , 2raz , 2rb0 , 2rb1 , 2rb2 , 2rbn , 2rbo , 2rbp , 2rbq , 2rbr , 2rbs , 3d3d , 3lzm , 4lzm , 5lzm , 6lzm , 7lzm
SCOP: d.2.1.3 , d.2.1.4
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Enzyme: EC:3.2.1.17
CAZy: GH24
PANDIT: PF00959
Blocks: IPB002196
Pfam Clan: CL0037.10

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR002196 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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P00720 Lysozyme

P76159 Probable lysozyme from lambdoid prophage Qin

Q556F2 Probable T4-type lysozyme 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002196 Glycoside hydrolase, family 24
IPR001165 Glycoside hydrolase, family 24, T4 lysozyme
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
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1. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995 [PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
2. Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995 [PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
3. Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
4. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
5. Weaver LH, Matthews BW.
Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution.
J. Mol. Biol. 193 189-99 1987 [PubMed: 3586019]
http://dx.doi.org/10.1016/0022-2836(87)90636-X
6. Faber HR, Matthews BW.
A mutant T4 lysozyme displays five different crystal conformations.
Nature 348 263-6 1990 [PubMed: 2234094]
http://dx.doi.org/10.1038/348263a0

Additional ReadingHelp
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Guo Z, Cascio D, Hideg K, Hubbell WL.
Structural determinants of nitroxide motion in spin-labeled proteins: solvent-exposed sites in helix B of T4 lysozyme.
Protein Sci. 17 2008 228-39 [PubMed: 18096642]
http://dx.doi.org/10.1110/ps.073174008
Collins MD, Quillin ML, Hummer G, Matthews BW, Gruner SM.
Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography.
J. Mol. Biol. 367 2007 752-63 [PubMed: 17292912]
http://dx.doi.org/10.1016/j.jmb.2006.12.021
Graves AP, Shivakumar DM, Boyce SE, Jacobson MP, Case DA, Shoichet BK.
Rescoring docking hit lists for model cavity sites: predictions and experimental testing.
J. Mol. Biol. 377 2008 914-34 [PubMed: 18280498]
http://dx.doi.org/10.1016/j.jmb.2008.01.049
Fleissner MR, Cascio D, Hubbell WL.
Structural origin of weakly ordered nitroxide motion in spin-labeled proteins.
Protein Sci. 18 2009 893-908 [PubMed: 19384990]
http://dx.doi.org/10.1002/pro.96
Guo Z, Cascio D, Hideg K, Kalai T, Hubbell WL.
Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme.
Protein Sci. 16 2007 1069-86 [PubMed: 17473014]
http://dx.doi.org/10.1110/ps.062739107
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