1fcq: Difference between revisions

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[[Image:1fcq.gif|left|200px]]
[[Image:1fcq.gif|left|200px]]


{{Structure
<!--
|PDB= 1fcq |SIZE=350|CAPTION= <scene name='initialview01'>1fcq</scene>, resolution 1.6&Aring;
The line below this paragraph, containing "STRUCTURE_1fcq", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Hyalurononglucosaminidase Hyalurononglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
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|DOMAIN=
{{STRUCTURE_1fcq| PDB=1fcq  | SCENE= }}  
|RELATEDENTRY=[[1fcu|1FCU]], [[1fcv|1FCV]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcq OCA], [http://www.ebi.ac.uk/pdbsum/1fcq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fcq RCSB]</span>
}}


'''CRYSTAL STRUCTURE (MONOCLINIC) OF BEE VENOM HYALURONIDASE'''
'''CRYSTAL STRUCTURE (MONOCLINIC) OF BEE VENOM HYALURONIDASE'''
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[[Category: Schirmer, T.]]
[[Category: Schirmer, T.]]
[[Category: Soldatova, L.]]
[[Category: Soldatova, L.]]
[[Category: 7-stranded (beta/alpha) tim barrel]]
[[Category: Allergen]]
[[Category: allergen]]
[[Category: Glycosidase family 56]]
[[Category: glycosidase family 56]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:10:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:20:23 2008''

Revision as of 16:10, 2 May 2008

File:1fcq.gif

Template:STRUCTURE 1fcq

CRYSTAL STRUCTURE (MONOCLINIC) OF BEE VENOM HYALURONIDASE


OverviewOverview

BACKGROUND: Hyaluronic acid (HA) is the most abundant glycosaminoglycan of vertebrate extracellular spaces and is specifically degraded by a beta-1,4 glycosidase. Bee venom hyaluronidase (Hya) shares 30% sequence identity with human hyaluronidases, which are involved in fertilization and the turnover of HA. On the basis of sequence similarity, mammalian enzymes and Hya are assigned to glycosidase family 56 for which no structure has been reported yet. RESULTS: The crystal structure of recombinant (Baculovirus) Hya was determined at 1.6 A resolution. The overall topology resembles a classical (beta/alpha)(8) TIM barrel except that the barrel is composed of only seven strands. A long substrate binding groove extends across the C-terminal end of the barrel. Cocrystallization with a substrate analog revealed the presence of a HA tetramer bound to subsites -4 to -1 and distortion of the -1 sugar. CONCLUSIONS: The structure of the complex strongly suggest an acid-base catalytic mechanism, in which Glu113 acts as the proton donor and the N-acetyl group of the substrate is the nucleophile. The location of the catalytic residues shows striking similarity to bacterial chitinase which also operates via a substrate-assisted mechanism.

About this StructureAbout this Structure

1FCQ is a Single protein structure of sequence from Apis mellifera. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of hyaluronidase, a major allergen of bee venom., Markovic-Housley Z, Miglierini G, Soldatova L, Rizkallah PJ, Muller U, Schirmer T, Structure. 2000 Oct 15;8(10):1025-35. PMID:11080624 Page seeded by OCA on Fri May 2 16:10:51 2008

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