5a8g: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
m Protected "5a8g" [edit=sysop:move=sysop]
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
==Crystal structure of the wild-type Staphylococcus aureus N- acetylneurminic acid lyase in complex with fluoropyruvate==
<StructureSection load='5a8g' size='340' side='right' caption='[[5a8g]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5a8g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A8G FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPF:N-(1-CARBOXY-2-FLUORO-ETHENYL)+LYSINE'>KPF</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8g OCA], [http://pdbe.org/5a8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a8g RCSB], [http://www.ebi.ac.uk/pdbsum/5a8g PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NANA_STAA8 NANA_STAA8]] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catalysis of reactions involving fluoropyruvate as donor by N-acetyl neuraminic acid lyase (NAL) variants was investigated. Under kinetic control, the wild-type enzyme catalysed the reaction between fluoropyruvate and N-acetyl mannosamine to give a 90 : 10 ratio of the (3R,4R)- and (3S,4R)-configured products; after extended reaction times, equilibration occurred to give a 30 : 70 mixture of these products. The efficiency and stereoselectivity of reactions of a range of substrates catalysed by the E192N, E192N/T167V/S208V and E192N/T167G NAL variants were also studied. Using fluoropyruvate and (2R,3S)- or (2S,3R)-2,3-dihydroxy-4-oxo-N,N-dipropylbutanamide as substrates, it was possible to obtain three of the four possible diastereomeric products; for each product, the ratio of anomeric and pyranose/furanose forms was determined. The crystal structure of S. aureus NAL in complex with fluoropyruvate was determined, assisting rationalisation of the stereochemical outcome of C-C bond formation.


The entry 5a8g is ON HOLD
Evaluation of fluoropyruvate as nucleophile in reactions catalysed by N-acetyl neuraminic acid lyase variants: scope, limitations and stereoselectivity.,Stockwell J, Daniels AD, Windle CL, Harman TA, Woodhall T, Lebl T, Trinh CH, Mulholland K, Pearson AR, Berry A, Nelson A Org Biomol Chem. 2015 Nov 5. PMID:26537532<ref>PMID:26537532</ref>


Authors: Stockwell, J., Daniels, A.D., Windle, C.L., Harman, T., Woodhall, T., Trinh, C.H., Lebel, T., Pearson, A.R., Mulholland, K., Berry, A., Nelson, A.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of the wild-type Staphylococcus aureus N-acetylneurminic acid lyase in complex with fluoropyruvate
<div class="pdbe-citations 5a8g" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
[[Category: Pearson, A.R]]
<references/>
__TOC__
</StructureSection>
[[Category: N-acetylneuraminate lyase]]
[[Category: Berry, A]]
[[Category: Daniels, A D]]
[[Category: Harman, T]]
[[Category: Lebel, T]]
[[Category: Lebel, T]]
[[Category: Trinh, C.H]]
[[Category: Mulholland, K]]
[[Category: Windle, C.L]]
[[Category: Nelson, A]]
[[Category: Pearson, A R]]
[[Category: Stockwell, J]]
[[Category: Stockwell, J]]
[[Category: Harman, T]]
[[Category: Trinh, C H]]
[[Category: Nelson, A]]
[[Category: Windle, C L]]
[[Category: Woodhall, T]]
[[Category: Woodhall, T]]
[[Category: Daniels, A.D]]
[[Category: Lyase]]
[[Category: Mulholland, K]]
[[Category: Berry, A]]
Retrieved from "https://proteopedia.org/5a8g"