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Volumn 56, Issue 2, 2004, Pages 396-400

Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 Å resolution

(43)  Spraggon, Glen a,c   Schwarzenbacher, Robert a,d   Kreusch, Andreas a,c   McMullan, Daniel a,c   Brinen, Linda S a,b   Canaves, Jaume M a,d   Dai, Xiaoping a,f   Deacon, Ashley M a,b   Elsliger, Marc André a,f   Eshagi, Said a,c   Floyd, Ross a,b   Godzik, Adam a,d   Grittini, Carina a,f   Grzechnik, Slawomir K a,d   Jaroszewski, Lukasz a,d   Karlak, Cathy a,c   Klock, Heath E a,c   Koesema, Eric a,c   Kovarik, John S a,b   Kuhn, Peter a,b   more..


Author keywords

[No Author keywords available]

Indexed keywords

METHIONYL AMINOPEPTIDASE;

EID: 3042724734     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20084     Document Type: Article
Times cited : (9)

References (12)
  • 1
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    • Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure
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    • (1987) J Bacteriol , vol.169 , pp. 751-757
    • Ben-Bassat, A.1    Bauer, K.2    Chang, S.Y.3    Myambo, K.4    Boosman, A.5    Chang, S.6
  • 2
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • Liu S, Widom J, Kemp CW, Crews CM, Clardy J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science 1998;282:1324-1327.
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Crews, C.M.4    Clardy, J.5
  • 4
    • 0033564306 scopus 로고    scopus 로고
    • Escherichia coli methionine aminopeptidase: Implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis
    • Lowther WT, Orville AM, Madden DT, Lim S, Rich DH, Matthews BW. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry 1999;38:7678-7688.
    • (1999) Biochemistry , vol.38 , pp. 7678-7688
    • Lowther, W.T.1    Orville, A.M.2    Madden, D.T.3    Lim, S.4    Rich, D.H.5    Matthews, B.W.6
  • 5
  • 6
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C. Dali: A network tool for protein structure comparison. Trends Biochem Sci 1995;20:478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 7
    • 0036081436 scopus 로고    scopus 로고
    • In search for more accurate alignments in the twilight zone
    • Jaroszewski L, Li W, Godzik A. In search for more accurate alignments in the twilight zone. Protein Sci 2002;11:1702-1713.
    • (2002) Protein Sci , vol.11 , pp. 1702-1713
    • Jaroszewski, L.1    Li, W.2    Godzik, A.3
  • 9
    • 0031059866 scopus 로고    scopus 로고
    • X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 Suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 12
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    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr D Biol Crystallogr 1991;47:110-119.
    • (1991) Acta Crystallogr D Biol Crystallogr , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.