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2md9

From Proteopedia

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Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein

Structural highlights

2md9 is a 1 chain structure with sequence from Brevibacillus parabrevis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TYCC_BREPA Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2md9"

@@ Line 4: / Line 4: @@
 == 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='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>
+</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 ==

2md9

From Proteopedia

Current revision

Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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