1fdz

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[[Image:1fdz.gif|left|200px]]
[[Image:1fdz.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1fdz |SIZE=350|CAPTION= <scene name='initialview01'>1fdz</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1fdz", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= NPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1fdz| PDB=1fdz | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdz OCA], [http://www.ebi.ac.uk/pdbsum/1fdz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fdz RCSB]</span>
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}}
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'''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION'''
'''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION'''
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[[Category: Pilling, P A.]]
[[Category: Pilling, P A.]]
[[Category: Smith, B J.]]
[[Category: Smith, B J.]]
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[[Category: aldolase]]
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[[Category: Aldolase]]
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[[Category: alpha-keto-acid lyase]]
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[[Category: Alpha-keto-acid lyase]]
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[[Category: carbon-carbon lyase]]
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[[Category: Carbon-carbon lyase]]
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[[Category: lyase]]
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[[Category: Lyase]]
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[[Category: oxo-acid lyase]]
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[[Category: Oxo-acid lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:13:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:21:09 2008''
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Revision as of 13:13, 2 May 2008

Image:1fdz.gif

Template:STRUCTURE 1fdz

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION


Overview

We describe here a sub-family of enzymes related both structurally and functionally to N-acetylneuraminate lyase. Two members of this family (N-acetylneuraminate lyase and dihydrodipicolinate synthase) have known three-dimensional structures and we now proceed to show their structural and functional relationship to two further proteins, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase and D-4-deoxy-5-oxoglucarate dehydratase. These enzymes are all thought to involve intermediate Schiff-base formation with their respective substrates. In order to understand the nature of this intermediate, we have determined the three-dimensional structure of N-acetylneuraminate lyase in complex with hydroxypyruvate (a product analogue) and in complex with one of its products (pyruvate). From these structures we deduce the presence of a closely similar Schiff-base forming motif in all members of the N-acetylneuraminate lyase sub-family. A fifth protein, MosA, is also confirmed to be a member of the sub-family although the involvement of an intermediate Schiff-base in its proposed reaction is unclear.

About this Structure

1FDZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase., Lawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM, J Mol Biol. 1997 Feb 21;266(2):381-99. PMID:9047371 Page seeded by OCA on Fri May 2 16:13:00 2008

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