4lzj

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(Difference between revisions)

Revision as of 13:06, 4 August 2016

Crystal Structure of MurQ from H.influenzae with bound inhibitor

Structural highlights

4lzj is a 4 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4m0d
Gene:	murQ ("Bacterium influenzae" Lehmann and Neumann 1896)
Activity:	N-acetylmuramic acid 6-phosphate etherase, with EC number 4.2.1.126
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MURQ_HAEIN] Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling (By similarity).

Publication Abstract from PubMed

The breakdown and recycling of peptidoglycan, an essential polymeric cell structure, occur in a number of bacterial species. A key enzyme in the recycling pathway of one of the components of the peptidoglycan layer, N-acetylmuramic acid (MurNAc), is MurNAc 6-phosphate hydrolase (MurQ). This enzyme catalyzes the cofactor-independent cleavage of a relatively nonlabile ether bond and presents an interesting target for mechanistic studies. Open chain product and substrate analogues were synthesized and tested as competitive inhibitors (Kis values of 1.1 +/- 0.3 and 0.23 +/- 0.02 mM, respectively) of the MurNAc 6P hydrolase from Escherichia coli (MurQ-EC). To identify the roles of active site residues that are important for catalysis, the substrate analogue was cocrystallized with the MurNAc 6P hydrolase from Haemophilus influenzae (MurQ-HI) that was amenable to crystallographic studies. The cocrystal structure of MurQ-HI with the substrate analogue showed that Glu89 was located in the proximity of both the C2 atom and the oxygen at the C3 position of the bound inhibitor and that no other potential acid/base residue that could act as an active site acid/base was located in the vicinity. The conserved residues Glu120 and Lys239 were found within hydrogen bonding distance of the C5 hydroxyl group and C6 phosphate group, suggesting that they play a role in substrate binding and ring opening. Combining these results with previous biochemical data, we propose a one-base mechanism of action in which Glu89 functions to both deprotonate at the C2 position and assist in the departure of the lactyl ether at the C3 position. This same residue would serve to deprotonate the incoming water and reprotonate the enolate in the second half of the catalytic cycle.

Structure of MurNAc 6-phosphate hydrolase (MurQ) from Haemophilus influenzae with a bound inhibitor.,Hadi T, Hazra S, Tanner ME, Blanchard JS Biochemistry. 2013 Dec 23;52(51):9358-66. doi: 10.1021/bi4010446. Epub 2013 Nov, 22. PMID:24251551^[1]

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

References

↑ Hadi T, Hazra S, Tanner ME, Blanchard JS. Structure of MurNAc 6-phosphate hydrolase (MurQ) from Haemophilus influenzae with a bound inhibitor. Biochemistry. 2013 Dec 23;52(51):9358-66. doi: 10.1021/bi4010446. Epub 2013 Nov, 22. PMID:24251551 doi:http://dx.doi.org/10.1021/bi4010446

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/4lzj"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of MurQ from H.influenzae with bound inhibitor==
 <StructureSection load='4lzj' size='340' side='right' caption='[[4lzj]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">murQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylmuramic_acid_6-phosphate_etherase N-acetylmuramic acid 6-phosphate etherase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.126 4.2.1.126] </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=4lzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lzj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lzj RCSB], [http://www.ebi.ac.uk/pdbsum/4lzj 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=4lzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lzj OCA], [http://pdbe.org/4lzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lzj RCSB], [http://www.ebi.ac.uk/pdbsum/4lzj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lzj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4lzj" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4lzj

From Proteopedia

Revision as of 13:06, 4 August 2016

Crystal Structure of MurQ from H.influenzae with bound inhibitor

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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