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| | {{STRUCTURE_1edt| PDB=1edt | SCENE= }} | | {{STRUCTURE_1edt| PDB=1edt | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION'''
| + | ===CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION=== |
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| - | ==Overview==
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| - | BACKGROUND: Endo-beta-N-acetylglucosaminidase H (Endo H), an endoglycosidase secreted by Streptomyces plicatus, hydrolyzes the glycosidic bond between the core N-acetyglucosamine residues of asparagine-linked high-mannose oligosaccharides. Endo H is a commonly used reagent in glycobiology research, including the characterization of oligosaccharides in glycoproteins. On-going crystallographic studies of Endo H and related endoglycosidases are aimed at identifying the molecular features that determine the different substrate specificities of these enzymes. RESULTS: The three-dimensional structure of Endo H has been determined to 1.9 A resolution. The overall fold of the enzyme is that of an irregular (alpha/beta)8-barrel comprising eight beta-strand/loop/alpha-helix units. Units 5 and 6 have very short loop sections at the top of the molecule and their alpha-helices are replaced by sections of extended geometry. The loop of unit 2 includes a small two-stranded antiparallel beta-sheet. A shallow curved cleft runs across the surface of the molecule from the area of units 5 and 6, over the core of the beta-barrel to the area of the beta-sheet of loop 2. This cleft contains the putative catalytic residues Asp130 and Glu132 above the core of the beta-barrel. These residues are surrounded by several aromatic residues. The loop 2 area of the cleft is formed by neutral polar residues, mostly asparagines. CONCLUSIONS: The structure of Endo H is very similar to that of Endo F1, a closely related endoglycosidase secreted by Flavobacterium meningosepticum. Detailed comparison of the structures of Endo H and Endo F1 supports the model previously proposed for substate binding and recognition, in which the area of loop 2 determines the substrate specificity and the alpha-helices of units 5 and 6 are missing to accommodate the protein moiety of the substrate.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7663942}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7663942 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7663942}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rao, V.]] | | [[Category: Rao, V.]] |
| | [[Category: Roey, P Van.]] | | [[Category: Roey, P Van.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:58:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:32:40 2008'' |
Revision as of 21:32, 30 June 2008
Template:STRUCTURE 1edt
CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION
Template:ABSTRACT PUBMED 7663942
About this Structure
1EDT is a Single protein structure of sequence from Streptomyces plicatus. Full crystallographic information is available from OCA.
Reference
Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 A resolution: active-site geometry and substrate recognition., Rao V, Guan C, Van Roey P, Structure. 1995 May 15;3(5):449-57. PMID:7663942
Page seeded by OCA on Tue Jul 1 00:32:40 2008
