6ckm: Difference between revisions

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<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=6ckm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ckm OCA], [http://pdbe.org/6ckm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ckm RCSB], [http://www.ebi.ac.uk/pdbsum/6ckm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ckm ProSAT]</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=6ckm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ckm OCA], [http://pdbe.org/6ckm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ckm RCSB], [http://www.ebi.ac.uk/pdbsum/6ckm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ckm ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytidine 5'-monophosphate (CMP)-sialic acid synthetase (CSS) is an essential enzyme involved in the biosynthesis of carbohydrates and glycoconjugates containing sialic acids, a class of alpha-keto acids that are generally terminal key recognition residues by many proteins that play important biological and pathological roles. The CSS from Neisseria meningitidis (NmCSS) has been commonly used with other enzymes such as sialic acid aldolase and/or sialyltransferase in synthesizing a diverse array of compounds containing sialic acid or its naturally occurring and non-natural derivatives. To better understand its catalytic mechanism and substrate promiscuity, four NmCSS crystal structures trapped at various stages of the catalytic cycle with bound substrates, substrate analogues, and products have been obtained and are presented here. These structures suggest a mechanism for an "open" and "closed" conformational transition that occurs as sialic acid binds to the NmCSS/cytidine-5'-triphosphate (CTP) complex. The closed conformation positions critical residues to help facilitate the nucleophilic attack of sialic acid C2-OH to the alpha-phosphate of CTP, which is also aided by two observed divalent cations. Product formation drives the active site opening, promoting the release of products.
Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography.,Matthews MM, McArthur JB, Li Y, Yu H, Chen X, Fisher AJ Biochemistry. 2019 Oct 4. doi: 10.1021/acs.biochem.9b00517. PMID:31583886<ref>PMID:31583886</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ckm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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Revision as of 13:11, 18 March 2020

N. meningitidis CMP-sialic acid synthetase in the presence of CMP-sialic acid and Ca2+N. meningitidis CMP-sialic acid synthetase in the presence of CMP-sialic acid and Ca2+

Structural highlights

6ckm is a 1 chain structure with sequence from "diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:neuA, siaB, synB ("Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887)
Activity:N-acylneuraminate cytidylyltransferase, with EC number 2.7.7.43
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Cytidine 5'-monophosphate (CMP)-sialic acid synthetase (CSS) is an essential enzyme involved in the biosynthesis of carbohydrates and glycoconjugates containing sialic acids, a class of alpha-keto acids that are generally terminal key recognition residues by many proteins that play important biological and pathological roles. The CSS from Neisseria meningitidis (NmCSS) has been commonly used with other enzymes such as sialic acid aldolase and/or sialyltransferase in synthesizing a diverse array of compounds containing sialic acid or its naturally occurring and non-natural derivatives. To better understand its catalytic mechanism and substrate promiscuity, four NmCSS crystal structures trapped at various stages of the catalytic cycle with bound substrates, substrate analogues, and products have been obtained and are presented here. These structures suggest a mechanism for an "open" and "closed" conformational transition that occurs as sialic acid binds to the NmCSS/cytidine-5'-triphosphate (CTP) complex. The closed conformation positions critical residues to help facilitate the nucleophilic attack of sialic acid C2-OH to the alpha-phosphate of CTP, which is also aided by two observed divalent cations. Product formation drives the active site opening, promoting the release of products.

Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography.,Matthews MM, McArthur JB, Li Y, Yu H, Chen X, Fisher AJ Biochemistry. 2019 Oct 4. doi: 10.1021/acs.biochem.9b00517. PMID:31583886[1]

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

References

  1. ↑ Matthews MM, McArthur JB, Li Y, Yu H, Chen X, Fisher AJ. Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography. Biochemistry. 2019 Oct 4. doi: 10.1021/acs.biochem.9b00517. PMID:31583886 doi:http://dx.doi.org/10.1021/acs.biochem.9b00517

6ckm, resolution 1.54Å

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