View source for 2md9


==Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein==
<StructureSection load='2md9' size='340' side='right'caption='[[2md9]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2md9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_parabrevis Brevibacillus parabrevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MD9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2md9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2md9 OCA], [https://pdbe.org/2md9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2md9 RCSB], [https://www.ebi.ac.uk/pdbsum/2md9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2md9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TYCC_BREPA TYCC_BREPA] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product.
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== Publication Abstract from PubMed ==
Phosphopantetheine transferases represent a class of enzymes found throughout all forms of life. From a structural point of view, they are subdivided into three groups, with transferases from group II being the most widespread. They are required for the posttranslational modification of carrier proteins involved in diverse metabolic pathways. We determined the crystal structure of the group II phosphopantetheine transferase Sfp from Bacillus in complex with a substrate carrier protein in the presence of coenzyme A and magnesium, and observed two protein-protein interaction sites. Mutational analysis showed that only the hydrophobic contacts between the carrier protein's second helix and the C-terminal domain of Sfp are essential for their productive interaction. Comparison with a similar structure of a complex of human proteins suggests that the mode of interaction is highly conserved in all domains of life.

Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification.,Tufar P, Rahighi S, Kraas FI, Kirchner DK, Lohr F, Henrich E, Kopke J, Dikic I, Guntert P, Marahiel MA, Dotsch V Chem Biol. 2014 Apr 2. pii: S1074-5521(14)00073-8. doi:, 10.1016/j.chembiol.2014.02.014. PMID:24704508<ref>PMID:24704508</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brevibacillus parabrevis]]
[[Category: Large Structures]]
[[Category: Dikic I]]
[[Category: Doetsch V]]
[[Category: Guentert P]]
[[Category: Henrich E]]
[[Category: Kirchner DK]]
[[Category: Koepke J]]
[[Category: Kraas FI]]
[[Category: Loehr F]]
[[Category: Marahiel MA]]
[[Category: Rahighi S]]
[[Category: Tufar P]]