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.


3spb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:03, 14 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3spb' size='340' side='right'caption='[[3spb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3spb' size='340' side='right'caption='[[3spb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3spb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Entcc Entcc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SPB FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3spb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae_subsp._cloacae_ATCC_13047 Enterobacter cloacae subsp. cloacae ATCC 13047]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SPB FirstGlance]. <br>
-
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ejd|1ejd]], [[1ejc|1ejc]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECL_04571, murA, murZ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=716541 ENTCC])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] </span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3spb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3spb OCA], [https://pdbe.org/3spb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3spb RCSB], [https://www.ebi.ac.uk/pdbsum/3spb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3spb ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3spb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3spb OCA], [https://pdbe.org/3spb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3spb RCSB], [https://www.ebi.ac.uk/pdbsum/3spb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3spb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/MURA_ENTCC MURA_ENTCC]] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.
+
[https://www.uniprot.org/uniprot/MURA_ENTCC MURA_ENTCC] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The enzyme MurA has been an established antibiotic target since the discovery of fosfomycin, which specifically inhibits MurA by covalent modification of the active site residue Cys115. Early biochemical studies established that Cys115 also covalently reacts with substrate phosphoenolpyruvate (PEP) to yield a phospholactoyl adduct, but the structural and functional consequences of this reaction remained obscure. We captured and depicted the Cys115-PEP adduct of E. cloacace MurA in various reaction states by X-ray crystallography. The data suggest that cellular MurA predominantly exists in a tightly locked complex with UDP-N-acetylmuramic acid (UNAM), the product of the MurB reaction, with PEP covalently attached to Cys115. The uniqueness and rigidity of this dormant complex was previously not recognized and presumably accounts for the failure of drug discovery efforts towards the identification of novel and effective MurA inhibitors. We demonstrate that recently published crystal structures of MurA from various organisms determined by different laboratories were indeed misinterpreted and actually contain UNAM and covalently bound PEP. The Cys115-PEP adduct was also captured in vitro during the reaction of free MurA and substrate UDP-N-acetylglucosamine (UNAG) or isomer UDP-N-acetylgalactosamine. The now available series of crystal structures allows a comprehensive view of the reaction cycle of MurA. It appears that the covalent reaction of MurA with PEP fulfills dual functions by tightening the complex with UNAM for the efficient feedback regulation of murein biosynthesis and by priming the PEP molecule for instantaneous reaction with substrate UNAG.
+
-
 
+
-
Functional consequence of the covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA).,Zhu JY, Yang Y, Han H, Betzi S, Olesen S, Marsilio F, Schonbrunn E J Biol Chem. 2012 Feb 29. PMID:22378791<ref>PMID:22378791</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3spb" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Entcc]]
+
[[Category: Enterobacter cloacae subsp. cloacae ATCC 13047]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]]
+
[[Category: Schonbrunn E]]
-
[[Category: Schonbrunn, E]]
+
[[Category: Yang Y]]
-
[[Category: Yang, Y]]
+
[[Category: Zhu J-Y]]
-
[[Category: Zhu, J Y]]
+
-
[[Category: Biogenesis/degradation]]
+
-
[[Category: Cell wall]]
+
-
[[Category: Mura]]
+
-
[[Category: Open enzyme state]]
+
-
[[Category: Peptidoglycan synthesis]]
+
-
[[Category: Transferase]]
+

Current revision

Unliganded E. Cloacae MurA

PDB ID 3spb

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/3spb"
Personal tools