Related ArticlesCrystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.
Structure. 2013 Jan 8;21(1):32-41
Authors: Nyirenda J, Matsumoto S, Saitoh T, Maita N, Noda NN, Inagaki F, Kohda D
Abstract
Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins. It possesses a binding pocket that recognizes Ser and Thr residues at the*+2 position in the*N-glycosylation consensus, Asn-X-Ser/Thr. We determined the crystal structures of the C-terminal globular domains of the catalytic subunits of two archaeal OSTs. A comparison with previously determined structures identified a segment with remarkable conformational plasticity, induced by crystal contact effects. We characterized its dynamic properties in solution by (15)N NMR relaxation analyses. Intriguingly, the mobile region contains the*+2 Ser/Thr-binding pocket. In agreement, the flexibility restriction forced by an engineered disulfide crosslink abolished the enzymatic activity, and its cleavage fully restored activity. These results suggest the necessity of multiple conformational states in the reaction. The dynamic nature of the Ser/Thr pocket could facilitate the efficient scanning of N-glycosylation sequons along nascent polypeptide chains.
[NMR paper] Crystallographic and NMR investigation of cobalt-substituted amicyanin.
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Biochemistry. 2004 Jul 27;43(29):9381-9
Authors: Carrell CJ, Wang X, Jones L, Jarrett WL, Davidson VL, Mathews FS
Cobalt(II) amicyanin was prepared by replacing the copper of the type I copper protein amicyanin from Paracoccus denitrificans with cobalt. The structure of the protein and the metal center have been characterized by X-ray crystallography and paramagnetic NMR spectroscopy....
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[NMR paper] Evidence for a strong hydrogen bond in the catalytic dyad of transition-state analogu
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J Am Chem Soc. 2002 Apr 24;124(16):4196-7
Authors: Westler WM, Frey PA, Lin J, Wemmer DE, Morimoto H, Williams PG, Markley JL
We present here the first accurate measurements of 1H (H) versus 3H (T) isotope...
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J Struct Biol. 2000 Aug;131(2):164-9
Authors: Hamdan S, Brown SE, Thompson PR, Yang JY, Carr PD, Ollis DL, Otting G, Dixon NE
The structured core of the N-terminal 3'-5' exonuclease domain of epsilon, the proofreading subunit of Escherichia coli DNA...
Crystallographic and NMR evaluation of the impact of peptide binding to the second PD
Crystallographic and NMR evaluation of the impact of peptide binding to the second PDZ domain of PTP1E.
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Biochemistry. 2010 Sep 14;
Authors: Zhang J, Sapienza PJ, Ke H, Chang A, Hengel SR, Wang H, Phillips GN, Lee AL
PDZ (PSD95/Discs large/ZO-1) domains are ubiquitous protein interaction motifs found in scaffolding proteins involved in signal transduction. Despite the fact that many PDZs show a limited tendency to undergo structural change, the...
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[NMR paper] Improving the quality of NMR and crystallographic protein structures by means of a co
Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases.
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Biochemistry. 1995 Nov 21;34(46):15351-8
Authors: Boerner RJ, Consler TG, Gampe RT, Weigl D, Willard DH, Davis DG, Edison AM, Loganzo F, Kassel DB, Xu RX
During solution...
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J Biol Buccale. 1990 Sep;18(3):189-94
Authors: Aoba T, Kawano K, Moreno EC
The present 1H-nmr study was undertaken to investigate the molecular structure of porcine amelogenins in solution using photo-CIDNP (chemically induced dynamic nuclear polarization). The proteins of interest...
Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.
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