1o78

From Proteopedia

(Difference between revisions)

@@ Line 1: / Line 1: @@
 ==Biotin carboxyl carrier domain of transcarboxylase (1.3S) [10-48] deletion mutant==
-<StructureSection load='1o78' size='340' side='right' caption='[[1o78]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1o78' size='340' side='right'caption='[[1o78]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1o78]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O78 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1o78]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O78 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dcz|1dcz]], [[1dd2|1dd2]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o78 OCA], [http://pdbe.org/1o78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o78 RCSB], [http://www.ebi.ac.uk/pdbsum/1o78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o78 ProSAT]</span></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=1o78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o78 OCA], [https://pdbe.org/1o78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o78 RCSB], [https://www.ebi.ac.uk/pdbsum/1o78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o78 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR]] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.
+[https://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Propionibacterium shermanii van niel 1928]]
+[[Category: Large Structures]]
-[[Category: Berger, S]]
+[[Category: Propionibacterium freudenreichii subsp. shermanii]]
-[[Category: Jank, M M]]
+[[Category: Berger S]]
-[[Category: Peikert, C]]
+[[Category: Jank MM]]
-[[Category: Sadowsky, J D]]
+[[Category: Peikert C]]
-[[Category: Carboxyl carrier]]
+[[Category: Sadowsky JD]]
-[[Category: Carrier protein]]
-[[Category: Transcarboxylase]]
-[[Category: Transferase]]

Current revision

Biotin carboxyl carrier domain of transcarboxylase (1.3S) [10-48] deletion mutant

spinqualitylabelsall models

PDB ID 1o78

Show:Asymmetric Unit Biological Assembly

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Structural highlights

1o78 is a 1 chain structure with sequence from Propionibacterium freudenreichii subsp. shermanii. 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

BCCP_PROFR The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A deletion mutant of the transcarboxylase biotin carrier protein was completely labeled with 13C and 15N. A multitude of 2D and 3D NMR spectra were recorded and assigned. An NMR solution structure was derived from the data and compared in detail with the recently published structure of the wild-type. It is shown that deletion of 30% of the amino acids does not alter the structure of the rigid protein core.

NMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit.,Jank MM, Sadowsky JD, Peikert C, Berger S Int J Biol Macromol. 2002 Oct 1;30(5):233-42. PMID:12297230^[1]

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

References

↑ Jank MM, Sadowsky JD, Peikert C, Berger S. NMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit. Int J Biol Macromol. 2002 Oct 1;30(5):233-42. PMID:12297230

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

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1o78

From Proteopedia

Current revision

Biotin carboxyl carrier domain of transcarboxylase (1.3S) [10-48] deletion mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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