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{{STRUCTURE_3h9j|  PDB=3h9j  |  SCENE=  }}
===Crystal structure of E. coli MccB + AMPCPP + SeMeT MccA===
{{ABSTRACT_PUBMED_19494832}}


==Function==
==Crystal structure of E. coli MccB + AMPCPP + SeMeT MccA==
[[http://www.uniprot.org/uniprot/MCCC7_ECOLX MCCC7_ECOLX]] Antibacterial peptide, active against enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, and strains of E.coli. Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp.<ref>PMID:2861788</ref> <ref>PMID:16574659</ref> <ref>PMID:18223070</ref> <ref>PMID:7559516</ref> <ref>PMID:17827970</ref> <ref>PMID:17711420</ref>
<StructureSection load='3h9j' size='340' side='right'caption='[[3h9j]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3h9j]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H9J FirstGlance]. <br>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3h9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h9j OCA], [https://pdbe.org/3h9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h9j RCSB], [https://www.ebi.ac.uk/pdbsum/3h9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h9j ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q47506_ECOLX Q47506_ECOLX]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/3h9j_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h9j ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 39-kDa Escherichia coli enzyme MccB catalyses a remarkable posttranslational modification of the MccA heptapeptide during the biosynthesis of microcin C7 (MccC7), a 'Trojan horse' antibiotic. The approximately 260-residue C-terminal region of MccB is homologous to ubiquitin-like protein (UBL) activating enzyme (E1) adenylation domains. Accordingly, MccB-catalysed C-terminal MccA-acyl-adenylation is reminiscent of the E1-catalysed activation reaction. However, unlike E1 substrates, which are UBLs with a C-terminal di-glycine sequence, MccB's substrate, MccA, is a short peptide with an essential C-terminal Asn. Furthermore, after an intramolecular rearrangement of MccA-acyl-adenylate, MccB catalyses a second, unique reaction, producing a stable phosphoramidate-linked analogue of acyl-adenylated aspartic acid. We report six-crystal structures of MccB in apo, substrate-, intermediate-, and inhibitor-bound forms. Structural and kinetic analyses reveal a novel-peptide clamping mechanism for MccB binding to heptapeptide substrates and a dynamic-active site for catalysing dual adenosine triphosphate-consuming reactions. The results provide insight into how a distinctive member of the E1 superfamily carries out two-step activation for generating the peptidyl-antibiotic MccC7.


==About this Structure==
How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.,Regni CA, Roush RF, Miller DJ, Nourse A, Walsh CT, Schulman BA EMBO J. 2009 Jul 8;28(13):1953-64. Epub 2009 Jun 4. PMID:19494832<ref>PMID:19494832</ref>
[[3h9j]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H9J OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:019494832</ref><references group="xtra"/><references/>
</div>
<div class="pdbe-citations 3h9j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Miller, D.]]
[[Category: Large Structures]]
[[Category: Nourse, A.]]
[[Category: Miller D]]
[[Category: Regni, C A.]]
[[Category: Nourse A]]
[[Category: Roush, R F.]]
[[Category: Regni CA]]
[[Category: Schulman, B A.]]
[[Category: Roush RF]]
[[Category: Walsh, C T.]]
[[Category: Schulman BA]]
[[Category: Antibiotic]]
[[Category: Walsh CT]]
[[Category: Antimicrobial]]
[[Category: Bacteriocin]]
[[Category: Formylation]]
[[Category: Mcc7]]
[[Category: Microcin]]
[[Category: N-p bond formation]]
[[Category: Peptide antibiotic]]
[[Category: Phosphoprotein]]
[[Category: Transferase]]
[[Category: Transferase-antibiotic complex]]
[[Category: Ubiquitin-activating enzyme]]
Retrieved from "https://proteopedia.org/3h9j"