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| | ==CRYSTAL STRUCTURE OF MURF LIGASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH ADP== | | ==CRYSTAL STRUCTURE OF MURF LIGASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH ADP== |
| - | <StructureSection load='3zl8' size='340' side='right' caption='[[3zl8]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='3zl8' size='340' side='right'caption='[[3zl8]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zl8]] is a 1 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=3ZL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZL8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zl8]] is a 1 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=3ZL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZL8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.65Å</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-tripeptide--D-alanyl-D-alanine_ligase UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.10 6.3.2.10] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3zl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zl8 OCA], [http://pdbe.org/3zl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zl8 RCSB], [http://www.ebi.ac.uk/pdbsum/3zl8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zl8 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=3zl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zl8 OCA], [https://pdbe.org/3zl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zl8 RCSB], [https://www.ebi.ac.uk/pdbsum/3zl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zl8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9WY78_THEMA Q9WY78_THEMA]] Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein (By similarity).[RuleBase:RU004136] | + | [https://www.uniprot.org/uniprot/Q9WY78_THEMA Q9WY78_THEMA] Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein (By similarity).[RuleBase:RU004136] |
| | <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: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine 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]]
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| - | [[Category: Atp-binding]]
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| - | [[Category: Cell cycle]]
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| - | [[Category: Cell division]]
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| - | [[Category: Cell shape]]
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| - | [[Category: Cell wall]]
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| - | [[Category: Ligase]]
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| - | [[Category: Nucleotide-binding]]
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| - | [[Category: Peptidoglycan synthesis]]
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| Structural highlights
Function
Q9WY78_THEMA Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein (By similarity).[RuleBase:RU004136]
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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