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New page: left|200px<br /><applet load="1fdy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdy, resolution 2.45Å" /> '''N-ACETYLNEURAMINATE ...
 
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[[Image:1fdy.gif|left|200px]]<br /><applet load="1fdy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fdy, resolution 2.45&Aring;" />
'''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE'''<br />


==Overview==
==N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE==
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.
<StructureSection load='1fdy' size='340' side='right'caption='[[1fdy]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fdy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FDY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdy OCA], [https://pdbe.org/1fdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fdy RCSB], [https://www.ebi.ac.uk/pdbsum/1fdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NANA_ECOLI NANA_ECOLI] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.[HAMAP-Rule:MF_01237]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fdy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fdy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:9047371</ref>
1FDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with 3PY as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FDY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9047371 9047371]
</div>
<div class="pdbe-citations 1fdy" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: N-acetylneuraminate lyase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Barbosa JARG]]
[[Category: Barbosa, J.A.R.G.]]
[[Category: Hall NE]]
[[Category: Hall, N.E.]]
[[Category: Lawrence MC]]
[[Category: Lawrence, M.C.]]
[[Category: Marcuccio SM]]
[[Category: Marcuccio, S.M.]]
[[Category: Ooi HC]]
[[Category: Ooi, H.C.]]
[[Category: Pilling PA]]
[[Category: Pilling, P.A.]]
[[Category: Smith BJ]]
[[Category: Smith, B.J.]]
[[Category: 3PY]]
[[Category: aldolase]]
[[Category: alpha-keto-acid lyase]]
[[Category: carbon-carbon lyase]]
[[Category: lyase]]
[[Category: oxo-acid lyase]]
 
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Latest revision as of 04:31, 17 October 2024

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE

1fdy, resolution 2.45Å

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