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| | <StructureSection load='4buc' size='340' side='right'caption='[[4buc]], [[Resolution|resolution]] 2.17Å' scene=''> | | <StructureSection load='4buc' size='340' side='right'caption='[[4buc]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4buc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4buc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.17Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bub|4bub]]</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=4buc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4buc OCA], [https://pdbe.org/4buc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4buc RCSB], [https://www.ebi.ac.uk/pdbsum/4buc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4buc ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanine--D-glutamate_ligase UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.9 6.3.2.9] </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=4buc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4buc OCA], [http://pdbe.org/4buc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4buc RCSB], [http://www.ebi.ac.uk/pdbsum/4buc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4buc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MURD_THEMA MURD_THEMA]] Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (By similarity). | + | [https://www.uniprot.org/uniprot/MURD_THEMA MURD_THEMA] Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Contreras-Martel, C]] | + | [[Category: Contreras-Martel C]] |
| - | [[Category: Dessen, A]] | + | [[Category: Dessen A]] |
| - | [[Category: Favini-Stabile, S]] | + | [[Category: Favini-Stabile S]] |
| - | [[Category: Thielens, N]] | + | [[Category: Thielens N]] |
| - | [[Category: Adp-forming enzyme]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Cell shape]]
| + | |
| - | [[Category: Cell wall]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Peptidoglycan synthesis]]
| + | |
| Structural highlights
4buc is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.17Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MURD_THEMA Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (By similarity).
Publication Abstract from PubMed
Peptidoglycan is a major determinant of cell shape in bacteria, and its biosynthesis involves the concerted action of cytoplasmic, membrane-associated and periplasmic enzymes. Within the cytoplasm, Mur enzymes catalyse the first steps leading to peptidoglycan precursor biosynthesis, and have been suggested as being part of a multicomponent complex that could also involve the transglycosylase MurG and the cytoskeletal protein MreB. In order to initialize the characterization of a potential Mur interaction network, we purified MurD, MurE, MurF, MurG and MreB from Thermotoga maritima and characterized their interactions using membrane blotting and surface plasmon resonance. MurD, MurE and MurF all recognize MurG and MreB, but not each other, while the two latter proteins interact. In addition, we solved the crystal structures of MurD, MurE and MurF, which indicate that their C-termini display high conformational flexibilities. The differences in Mur conformations could be important parameters for the stability of an intracytoplasmic murein biosynthesis complex.
MreB and MurG as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis.,Favini-Stabile S, Contreras-Martel C, Thielens N, Dessen A Environ Microbiol. 2013 Jun 3. doi: 10.1111/1462-2920.12171. PMID:23826965[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Favini-Stabile S, Contreras-Martel C, Thielens N, Dessen A. MreB and MurG as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis. Environ Microbiol. 2013 Jun 3. doi: 10.1111/1462-2920.12171. PMID:23826965 doi:10.1111/1462-2920.12171
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