This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5a8g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5a8g" [edit=sysop:move=sysop])
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]]
+

Revision as of 18:58, 1 December 2015

Crystal structure of the wild-type Staphylococcus aureus N- acetylneurminic acid lyase in complex with fluoropyruvate

5a8g, resolution 1.72Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5a8g"
Personal tools