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4imd

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Revision as of 16:22, 5 August 2016

Crystal Structure of Pasteurella multocida N-Acetyl-D-Neuraminic acid lyase trapped with pyruvate covalently bound through a Schiff base to Lys164

Structural highlights

4imd is a 4 chain structure with sequence from Pasteurella multocida subsp. gallicida p1059. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	4imc, 4ime, 4imf, 4img
Gene:	nanA, PM1715 (Pasteurella multocida subsp. gallicida P1059)
Activity:	N-acetylneuraminate lyase, with EC number 4.1.3.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NANA_PASMU] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (By similarity).

Publication Abstract from PubMed

N-Acetylneuraminate lyases (NALs) or sialic acid aldolases catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac, the most common form of sialic acid) to form pyruvate and N-acetyl-D-mannosamine (ManNAc). Although equilibrium favors sialic acid cleavage, these enzymes can be used for high-yield chemoenzymatic synthesis of structurally diverse sialic acids in the presence of excess pyruvate. Engineering these enzymes to synthesize structurally modified natural sialic acids and their non-natural derivatives holds promise in creating novel therapeutic agents. Atomic resolution structures of these enzymes will greatly assist in guiding mutagenic and modeling studies to engineer enzymes with altered substrate specificity. We report here the crystal structures of wild-type Pasteurella multocida N-acetylneuraminate lyase and its K164A mutant. Like other bacterial lyases, it assembles into a homotetramer with each monomer folding into a classic (beta/alpha)8 TIM barrel. Two wild-type structures were determined; in the absence of substrates, and trapped in a Schiff base intermediate between Lys164 and pyruvate, respectively. Three structures of the K164A variant were determined: one in the absence of substrates and two binary complexes with N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), respectively. Both sialic acids bind to the active site in the open-chain ketone form of the monosaccharide. The structures reveal that every hydroxyl group of the linear sugars makes hydrogen bond interactions with the enzyme and the residues that determine specificity were identified. Additionally, the structures lend some clues in explaining the natural discrimination of sialic acid substrates between the P. multocida and E. coli NALs.

Structural basis for substrate specificity and mechanism of N-acetyl-D-neuraminic acid lyase from Pasteurella multocida.,Huynh N, Aye A, Li Y, Yu H, Cao H, Tiwari VK, Shin DW, Chen X, Fisher AJ Biochemistry. 2013 Oct 23. PMID:24152047^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Huynh N, Aye A, Li Y, Yu H, Cao H, Tiwari VK, Shin DW, Chen X, Fisher AJ. Structural basis for substrate specificity and mechanism of N-acetyl-D-neuraminic acid lyase from Pasteurella multocida. Biochemistry. 2013 Oct 23. PMID:24152047 doi:http://dx.doi.org/10.1021/bi4011754

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4imd"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Pasteurella multocida N-Acetyl-D-Neuraminic acid lyase trapped with pyruvate covalently bound through a Schiff base to Lys164==
 <StructureSection load='4imd' size='340' side='right' caption='[[4imd]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 8: / Line 9: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nanA, PM1715 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1169409 Pasteurella multocida subsp. gallicida P1059])</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=4imd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4imd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4imd RCSB], [http://www.ebi.ac.uk/pdbsum/4imd PDBsum]</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=4imd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4imd OCA], [http://pdbe.org/4imd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4imd RCSB], [http://www.ebi.ac.uk/pdbsum/4imd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4imd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 20: / Line 21: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4imd" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4imd

From Proteopedia

Revision as of 16:22, 5 August 2016

Crystal Structure of Pasteurella multocida N-Acetyl-D-Neuraminic acid lyase trapped with pyruvate covalently bound through a Schiff base to Lys164

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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