001     85680
005     20250731122903.0
024 7 _ |a pmid:17963237
|2 pmid
024 7 _ |a 10.1002/prot.21700
|2 doi
024 7 _ |a 0887-3585
|2 ISSN
024 7 _ |a 1097-0134
|2 ISSN
024 7 _ |a WOS:000254263400005
|2 WOS
024 7 _ |a openalex:W2042323571
|2 openalex
037 _ _ |a PHPPUBDB-8387
041 _ _ |a eng
082 _ _ |a 540
100 1 _ |a Matrai, J.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study
260 _ _ |a New York, NY
|b Wiley-Liss
|c 2008
300 _ _ |a 552-564
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a article
|2 DRIVER
336 7 _ |a Journal Article
|m journal
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
440 _ 0 |a Proteins: Struct. Funct. Bioinf.
|v 71
|y 2
|x 0887-3585
|0 PERI:(DE-600)1475032-6
500 _ _ |3 Converted on 2013-05-30 12:31
500 _ _ |3 Converted on 2013-06-21 19:20
520 _ _ |a In the present study, we report on the X-ray crystallographic structure of a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This structure was solved to reveal the features of sugar binding in the catalytic pocket. However, as demonstrated by the X-ray structure the sugar binding and the catalytic pocket arrangement is significantly altered as compared with what was expected based on previous X-ray structures on GH-J clan enzymes. We performed a series of docking and molecular dynamics simulations on various derivatives of AtcwINV1 to reveal the reasons behind this modified sugar binding. Our results demonstrate that the E203Q mutation introduced into the catalytic pocket triggers conformational changes that alter the wild type substrate binding. In addition, this study also reveals the putative productive sucrose binding modus in the wild type enzyme.
536 _ _ |0 G:(DE-H253)POF1-No-Ref-20130405
|f POF I
|x 0
|c POF1-550
|a FS Beamline without reference (POF1-550)
588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Substitution
650 _ 2 |2 MeSH
|a Arabidopsis: enzymology
650 _ 2 |2 MeSH
|a Computer Simulation
650 _ 2 |2 MeSH
|a Crystallization
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Protein Conformation: drug effects
650 _ 2 |2 MeSH
|a Sucrose: metabolism
650 _ 2 |2 MeSH
|a beta-Fructofuranosidase: chemistry
650 _ 2 |2 MeSH
|a beta-Fructofuranosidase: genetics
650 _ 2 |2 MeSH
|a beta-Fructofuranosidase: metabolism
650 _ 7 |0 57-50-1
|2 NLM Chemicals
|a Sucrose
650 _ 7 |0 EC 3.2.1.26
|2 NLM Chemicals
|a beta-Fructofuranosidase
693 _ _ |0 EXP:(DE-H253)Unknown-BL-20150101
|f Unknown DESY Beamline
|x 0
|6 EXP:(DE-H253)Unknown-BL-20150101
700 1 _ |a Lammens, W.
700 1 _ |a Jonckheer, A.
700 1 _ |a Le Roy, K.
700 1 _ |a Rabijns, A.
700 1 _ |a Van den Ende, W.
700 1 _ |a De Maeyer, M.
773 _ _ |0 PERI:(DE-600)1475032-6
|a 10.1002/prot.21700
|g Vol. 71, p. 552-564
|p 552-564
|q 71<552-564
|t Proteins
|v 71
|x 0887-3585
|y 2008
856 4 0 |u http://www3.interscience.wiley.com/cgi-bin/fulltext/116835267/PDFSTART
909 C O |o oai:bib-pubdb1.desy.de:85680
|p VDB
910 1 _ |0 I:(DE-HGF)0
|a Externes Institut
|k Extern
913 1 _ |0 G:(DE-HGF)POF1-540
|9 G:(DE-H253)POF1-No-Ref-20130405
|v Kondensierte Materie
|x 0
|a DE-H253
|4 G:(DE-HGF)POF
|1 G:(DE-HGF)POF1-550
|3 G:(DE-HGF)POF1
|2 G:(DE-HGF)POF1-500
|b Struktur der Materie
|l Großgeräte für die Forschung mit Photonen, Neutronen, Ionen
914 1 _ |a (c) 2008 Wiley-Liss, Inc., A Wiley Company
|y 2008
915 _ _ |a JCR/ISI refereed
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915 _ _ |a JCR
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915 _ _ |a No Author Disambiguation
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920 _ 1 |k EMBL
|i European Molecular Biology Laboratory
920 1 _ |0 I:(DE-H253)EMBL_-2012_-20130307
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|l European Molecular Biology Laboratory
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920 _ _ |k 001
980 _ _ |a PHPPUBDB
980 _ _ |a VDB
980 _ _ |a UNRESTRICTED
980 _ _ |a journal
980 _ _ |a I:(DE-H253)EMBL_-2012_-20130307
980 _ _ |a ConvertedRecord


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