메뉴 건너뛰기




Volumn 14, Issue 3-4, 2001, Pages 271-313

Zinc coordination sphere in biochemical zinc sites

Author keywords

Crystal structure; Metalloenzyme; NMR; Protein sequence; X ray crystallography; XAFS or X ray absorption fine structure

Indexed keywords

ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME; ALCOHOL DEHYDROGENASE; AMINO ACID TRANSFER RNA LIGASE; AMINOPEPTIDASE; ASPARTIC ACID; ASTACIN; BETA LACTAMASE; CARBONATE DEHYDRATASE; CARBOXYPEPTIDASE; CYSTEINE; GLUTAMIC ACID; HISTIDINE; MATRIX METALLOPROTEINASE; METALLOPROTEIN; NITRIC OXIDE SYNTHASE; NITROGEN; PHOSPHATASE; PHOSPHOTRIESTERASE; PROTEIN KINASE; SULFUR; SUPERANTIGEN; SUPEROXIDE DISMUTASE; THERMOLYSIN; UNCLASSIFIED DRUG; WATER; ZINC; ZINC PROTEIN;

EID: 0035690880     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1012976615056     Document Type: Review
Times cited : (631)

References (357)
  • 7
    • 0001786996 scopus 로고
    • Acyl group transfer- metalloproteinases
    • Page MI, Williams A, ed. London: Royal Society of Chemistry Burlington House
    • (1987) Enzyme Mechanisms , pp. 241-258
    • Auld, D.S.1
  • 22
    • 0028027226 scopus 로고
    • Crystal structure of the 50 kDa metallo protease from Serratia marcescens
    • (1994) J Mol Biol , vol.242 , pp. 244-251
    • Baumann, U.1
  • 24
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • (1993) EMBO J , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 29
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 46
    • 0028971611 scopus 로고
    • 6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding
    • (1995) J Mol Biol , vol.253 , pp. 358-369
    • Burgisser, D.M.1    Thony, B.2    Redweik, U.3    Hess, D.4    Heizmann, C.W.5    Huber, R.6    Nar, H.7
  • 58
    • 0031439461 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active site glutamate in human matrilysin: Investigation of its role in catalysis
    • (1997) Biochemistry , vol.36 , pp. 16019-16024
    • Cha, J.1    Auld, D.S.2
  • 67
    • 0034720771 scopus 로고    scopus 로고
    • Inhibition of carboxypeptidase A by D-pencillamine: Mechanism and implications for drug design
    • (2000) Biochemistry , vol.39 , pp. 7580-7588
    • Chong, C.R.1    Auld, D.S.2
  • 88
    • 0029942857 scopus 로고    scopus 로고
    • Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure
    • (1996) J Mol Biol , vol.259 , pp. 458-466
    • Dreyer, M.K.1    Schulz, G.E.2
  • 112
    • 0027275248 scopus 로고
    • Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins
    • (1993) J Mol Biol , vol.231 , pp. 1078-1089
    • Fourmy, D.1    Dardel, F.2    Blanquet, S.3
  • 118
    • 0023192209 scopus 로고
    • Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 Å resolution
    • (1987) J Mol Biol , vol.195 , pp. 373-396
    • Fujinaga, M.1    James, M.N.2
  • 122
    • 0032829746 scopus 로고    scopus 로고
    • Significance of metal ions in galactose-1-phosphate uridylyltransferase: An essential: Structural zinc and a nonessential structural iron
    • (1999) Biochemistry , vol.38 , pp. 13398-13406
    • Geeganage, S.1    Frey, P.A.2
  • 137
    • 0026548881 scopus 로고
    • Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation
    • (1992) J Mol Biol , vol.224 , pp. 141-157
    • Guasch, A.1    Coll, M.2    Aviles, F.X.3    Huber, R.4
  • 163
    • 0039710379 scopus 로고    scopus 로고
    • Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: Molecular explanations for X-linked agammaglobulinaemia
    • (1997) EMBO J , vol.16 , pp. 3396-3404
    • Hyvonen, M.1    Saraste, M.2
  • 167
  • 173
    • 0026571013 scopus 로고
    • Identification of HLA-DR1 beta chain residues critical for binding staphylococcal enterotoxins A and E
    • (1992) J Exp Med , vol.175 , pp. 415-424
    • Karp, D.R.1    Long, E.O.2
  • 175
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis
    • (1991) J Mol Biol , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 177
    • 0034599484 scopus 로고    scopus 로고
    • The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases
    • (2000) EMBO J , vol.19 , pp. 1407-1418
    • Kimber, M.S.1    Pai, E.F.2
  • 184
    • 0032701795 scopus 로고    scopus 로고
    • Zinc finger peptides for the regulation of gene expression
    • (1999) J Mol Bio1 , vol.293 , pp. 215-218
    • Klug, A.1
  • 185
  • 188
    • 0034697988 scopus 로고    scopus 로고
    • The structure of rhamnose isomerase from Escherichia coil and its relation with xylose isomerase illustrates a change between inter and intrasubunit complementation during evolution
    • (2000) J Mol Biol , vol.300 , pp. 917-933
    • Korndorfer, I.P.1    Fessner, W.D.2    Matthews, B.W.3
  • 203
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 218
    • 0024822481 scopus 로고
    • Cobalt(II-substituted class III alcohol and sorbitol dehydrogenases from human liver
    • (1989) Biochemistry , vol.28 , pp. 9944-9949
    • Maret, W.1
  • 221
    • 0022448449 scopus 로고
    • Influence of anions and pH on the conformational change of horse liver alcohol dehydrogenase induced by binding of oxidized nicotinamide adenine dinucleotide: Binding of chloride to the catalytic metal ion
    • (1986) Biochemistry , vol.25 , pp. 1584-1588
    • Maret, W.1    Zeppezauer, M.2
  • 225
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc proteases
    • (1988) Acc Chem Res , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 244
    • 0034653865 scopus 로고    scopus 로고
    • Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase
    • (2000) Structure , vol.8 , pp. 231-239
    • Pan, H.1    Wigley, D.B.2
  • 269
    • 0025173275 scopus 로고
    • Immunochemical characterization of antigenic domains on human interferon-beta: Spatially distinct epitopes are associated with both antiviral and antiproliferative activities
    • (1990) Eur J Immunol , vol.20 , pp. 1933-1939
    • Redlich, P.N.1    Grossberg, S.E.2
  • 278
    • 0029033663 scopus 로고
    • On the role of Glu-68 in alcohol dehydrogenase
    • (1995) Protein Sci , vol.4 , pp. 1124-1132
    • Ryde, U.1
  • 297
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 305
    • 0029116127 scopus 로고
    • Transition state analogue Lleucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65Å resolution in a new crystal form
    • (1995) Biochemistry , vol.34 , pp. 9200-9210
    • Strater, N.1    Lipscomb, W.N.2
  • 317
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • (1993) FASEB J , vol.7 , pp. 290-298
    • Taylor, A.1
  • 341
    • 0032499630 scopus 로고    scopus 로고
    • Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity
    • (1998) Biochemistry , vol.37 , pp. 8314-8324
    • Wang, Z.1    Quiocho, F.A.2
  • 343
    • 0027398949 scopus 로고
    • A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
    • (1993) Biochemistry , vol.32 , pp. 1689-1694
    • Wilson, D.K.1    Quiocho, F.A.2
  • 344
  • 357
    • 0033229964 scopus 로고    scopus 로고
    • Structure of acutolysin-C, a haemorrhagic toxin from the venom of Agkistrodon acutus, providing further evidence for the mechanism of the pH-dependent proteolytic reaction of zinc metalloproteinases
    • (1999) Acta Crystallogr D Biol Cryst , vol.55 , pp. 1834-1841
    • Zhu, X.1    Teng, M.2    Niu, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.