1m1k

<StructureSection load='1m1k' size='340' side='right' caption='[[1m1k]], [[Resolution|resolution]] 3.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1m1k]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1K FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZIT:AZITHROMYCIN'>ZIT</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k73|1k73]], [[1k8a|1k8a]], [[1k9m|1k9m]], [[1kc8|1kc8]], [[1kd1|1kd1]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m1k RCSB], [http://www.ebi.ac.uk/pdbsum/1m1k PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1k_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Crystal structures of the Haloarcula marismortui large ribosomal subunit complexed with the 16-membered macrolide antibiotics carbomycin A, spiramycin, and tylosin and a 15-membered macrolide, azithromycin, show that they bind in the polypeptide exit tunnel adjacent to the peptidyl transferase center. Their location suggests that they inhibit protein synthesis by blocking the egress of nascent polypeptides. The saccharide branch attached to C5 of the lactone rings extends toward the peptidyl transferase center, and the isobutyrate extension of the carbomycin A disaccharide overlaps the A-site. Unexpectedly, a reversible covalent bond forms between the ethylaldehyde substituent at the C6 position of the 16-membered macrolides and the N6 of A2103 (A2062, E. coli). Mutations in 23S rRNA that result in clinical resistance render the binding site less complementary to macrolides.

The structures of four macrolide antibiotics bound to the large ribosomal subunit.,Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB, Steitz TA Mol Cell. 2002 Jul;10(1):117-28. PMID:12150912<ref>PMID:12150912</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[User:Wayne Decatur/Haloarcula Large Ribosomal Subunit With Azithromycin|User:Wayne Decatur/Haloarcula Large Ribosomal Subunit With Azithromycin]]

== References ==

<references/>

[[Category: Ban, N.]]

[[Category: Hansen, J L.]]

[[Category: Ippolito, J A.]]

[[Category: Moore, P B.]]

[[Category: Nissen, P.]]

[[Category: Steitz, T A.]]

[[Category: Ribosome]]