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| | <StructureSection load='3rum' size='340' side='right'caption='[[3rum]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='3rum' size='340' side='right'caption='[[3rum]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rum]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_lurida Amycolatopsis lurida] and [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RUM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rum]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_lurida Amycolatopsis lurida] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RUM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=RST:RISTOSAMINE'>RST</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=BXY:ALPHA-D-ARABINOFURANOSE'>BXY</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</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]] 1.851Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=HTY:(BETAR)-BETA-HYDROXY-D-TYROSINE'>HTY</scene>, <scene name='pdbligand=MDF:META,+META-DI-HYDROXY-PHENYLALANINE'>MDF</scene>, <scene name='pdbligand=MP4:(2S)-AMINO(3,5-DIHYDROXY-4-METHYLPHENYL)ETHANOIC+ACID'>MP4</scene>, <scene name='pdbligand=OMX:(BETAR)-BETA-HYDROXY-L-TYROSINE'>OMX</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BXY:ALPHA-D-ARABINOFURANOSE'>BXY</scene>, <scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HTY:(BETAR)-BETA-HYDROXY-D-TYROSINE'>HTY</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MDF:META,+META-DI-HYDROXY-PHENYLALANINE'>MDF</scene>, <scene name='pdbligand=MP4:(2S)-AMINO(3,5-DIHYDROXY-4-METHYLPHENYL)ETHANOIC+ACID'>MP4</scene>, <scene name='pdbligand=OMX:(BETAR)-BETA-HYDROXY-L-TYROSINE'>OMX</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene>, <scene name='pdbligand=RST:RISTOSAMINE'>RST</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1anf|1anf]], [[3rul|3rul]], [[3run|3run]], [[3vfj|3vfj]], [[3vfk|3vfk]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, b4034, JW3994 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3rum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rum OCA], [https://pdbe.org/3rum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rum RCSB], [https://www.ebi.ac.uk/pdbsum/3rum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rum 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=3rum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rum OCA], [https://pdbe.org/3rum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rum RCSB], [https://www.ebi.ac.uk/pdbsum/3rum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rum ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
| + | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 29: |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Amycolatopsis lurida]] | | [[Category: Amycolatopsis lurida]] |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Economou, N J]] | + | [[Category: Economou NJ]] |
| - | [[Category: Grasty, K C]] | + | [[Category: Grasty KC]] |
| - | [[Category: Loll, P J]] | + | [[Category: Loll PJ]] |
| - | [[Category: Nahoum, V]] | + | [[Category: Nahoum V]] |
| - | [[Category: Weeks, S D]] | + | [[Category: Weeks SD]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Carboxymethylation of cysteine]]
| + | |
| - | [[Category: Fusion]]
| + | |
| - | [[Category: Glycopeptide]]
| + | |
| - | [[Category: Native protein ligation]]
| + | |
| - | [[Category: Ristocetin]]
| + | |
| - | [[Category: Sugar binding protein-antibiotic complex]]
| + | |
| Structural highlights
3rum is a 3 chain structure with sequence from Amycolatopsis lurida and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.851Å |
| Ligands: | , , , , , , , , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
Publication Abstract from PubMed
Many large natural product antibiotics act by specifically binding and sequestering target molecules found on bacterial cells. We have developed a new strategy to expedite the structural analysis of such antibiotic-target complexes, in which we covalently link the target molecules to carrier proteins, and then crystallize the entire carrier-target-antibiotic complex. Using native chemical ligation, we have linked the Lys-D-Ala-D-Ala binding epitope for glycopeptide antibiotics to three different carrier proteins. We show that recognition of this peptide by multiple antibiotics is not compromised by the presence of the carrier protein partner, and use this approach to determine the first-ever crystal structure for the new therapeutic dalbavancin. We also report the first crystal structure of an asymmetric ristocetin antibiotic dimer, as well as the structure of vancomycin bound to a carrier-target fusion. The dalbavancin structure reveals an antibiotic molecule that has closed around its binding partner; it also suggests mechanisms by which the drug can enhance its half-life by binding to serum proteins, and be targeted to bacterial membranes. Notably, the carrier protein approach is not limited to peptide ligands such as Lys-D-Ala-D-Ala, but is applicable to a diverse range of targets. This strategy is likely to yield structural insights that accelerate new therapeutic development.
A carrier protein strategy yields the structure of dalbavancin.,Economou NJ, Nahoum V, Weeks SD, Grasty KC, Zentner IJ, Townsend TM, Bhuiya MW, Cocklin S, Loll PJ J Am Chem Soc. 2012 Mar 14;134(10):4637-45. Epub 2012 Mar 1. PMID:22352468[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Economou NJ, Nahoum V, Weeks SD, Grasty KC, Zentner IJ, Townsend TM, Bhuiya MW, Cocklin S, Loll PJ. A carrier protein strategy yields the structure of dalbavancin. J Am Chem Soc. 2012 Mar 14;134(10):4637-45. Epub 2012 Mar 1. PMID:22352468 doi:10.1021/ja208755j
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