2md9

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{{STRUCTURE_2md9| PDB=2md9 | SCENE= }}
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==Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein==
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===Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein===
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<StructureSection load='2md9' size='340' side='right' caption='[[2md9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_24704508}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2md9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10027 Atcc 10027]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MD9 OCA]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gdy|2gdy]], [[2gdx|2gdx]], [[2gdw|2gdw]], [[2ge1|2ge1]], [[1dny|1dny]], [[4mrt|4mrt]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tycC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 ATCC 10027])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<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=2md9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2md9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2md9 RCSB], [http://www.ebi.ac.uk/pdbsum/2md9 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Function==
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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>
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[[http://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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==About this Structure==
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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[[2md9]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MD9 OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:024704508</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
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[[Category: Atcc 10027]]
[[Category: Dikic, I.]]
[[Category: Dikic, I.]]
[[Category: Doetsch, V.]]
[[Category: Doetsch, V.]]

Revision as of 06:55, 14 May 2014

Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein

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