2bb6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:52, 30 October 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2bb6.gif|left|200px]]
 
-
{{Structure
+
==Structure of Cobalamin-complexed Bovine Transcobalamin in Monoclinic Crystal Form==
-
|PDB= 2bb6 |SIZE=350|CAPTION= <scene name='initialview01'>2bb6</scene>, resolution 2.00&Aring;
+
<StructureSection load='2bb6' size='340' side='right'caption='[[2bb6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
+
<table><tr><td colspan='2'>[[2bb6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BB6 FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-
|GENE= TCN2, TC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bb6 OCA], [https://pdbe.org/2bb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bb6 RCSB], [https://www.ebi.ac.uk/pdbsum/2bb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bb6 ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[2bb5|2BB5]], [[2bbc|2BBC]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bb6 OCA], [http://www.ebi.ac.uk/pdbsum/2bb6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bb6 RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/TCO2_BOVIN TCO2_BOVIN] Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.
-
 
+
== Evolutionary Conservation ==
-
'''Structure of Cobalamin-complexed Bovine Transcobalamin in Monoclinic Crystal Form'''
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==Overview==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/2bb6_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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/main_output.php?pdb_ID=2bb6 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
Cobalamin (Cbl, vitamin B(12)) serves for two essential cofactors in mammals. The pathway for its intestinal absorption, plasma transport, and cellular uptake uses cell surface receptors and three Cbl-transporting proteins, haptocorrin, intrinsic factor, and transcobalamin (TC). We present the structure determination of a member of the mammalian Cbl-transporter family. The crystal structures of recombinant human and bovine holo-TCs reveal a two-domain architecture, with an N-terminal alpha(6)-alpha(6) barrel and a smaller C-terminal domain. One Cbl molecule in base-on conformation is buried inside the domain interface. Structural data combined with previous binding assays indicate a domain motion in the first step of Cbl binding. In a second step, the weakly coordinated ligand H(2)O at the upper axial side of added H(2)O-Cbl is displaced by a histidine residue of the alpha(6)-alpha(6) barrel. Analysis of amino acid conservation on TC's surface in orthologous proteins suggests the location of the TC-receptor-recognition site in an extended region on the alpha(6)-alpha(6) barrel. The TC structure allows for the mapping of sites of amino acid variation due to polymorphisms of the human TC gene. Structural information is used to predict the overall fold of haptocorrin and intrinsic factor and permits a rational approach to the design of new Cbl-based bioconjugates for diagnostic or therapeutic drug delivery.
Cobalamin (Cbl, vitamin B(12)) serves for two essential cofactors in mammals. The pathway for its intestinal absorption, plasma transport, and cellular uptake uses cell surface receptors and three Cbl-transporting proteins, haptocorrin, intrinsic factor, and transcobalamin (TC). We present the structure determination of a member of the mammalian Cbl-transporter family. The crystal structures of recombinant human and bovine holo-TCs reveal a two-domain architecture, with an N-terminal alpha(6)-alpha(6) barrel and a smaller C-terminal domain. One Cbl molecule in base-on conformation is buried inside the domain interface. Structural data combined with previous binding assays indicate a domain motion in the first step of Cbl binding. In a second step, the weakly coordinated ligand H(2)O at the upper axial side of added H(2)O-Cbl is displaced by a histidine residue of the alpha(6)-alpha(6) barrel. Analysis of amino acid conservation on TC's surface in orthologous proteins suggests the location of the TC-receptor-recognition site in an extended region on the alpha(6)-alpha(6) barrel. The TC structure allows for the mapping of sites of amino acid variation due to polymorphisms of the human TC gene. Structural information is used to predict the overall fold of haptocorrin and intrinsic factor and permits a rational approach to the design of new Cbl-based bioconjugates for diagnostic or therapeutic drug delivery.
-
==About this Structure==
+
Structural basis for mammalian vitamin B12 transport by transcobalamin.,Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4386-91. Epub 2006 Mar 14. PMID:16537422<ref>PMID:16537422</ref>
-
2BB6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB6 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structural basis for mammalian vitamin B12 transport by transcobalamin., Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4386-91. Epub 2006 Mar 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16537422 16537422]
+
</div>
 +
<div class="pdbe-citations 2bb6" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Fedosov, S N.]]
+
[[Category: Fedosov SN]]
-
[[Category: Garau, G.]]
+
[[Category: Garau G]]
-
[[Category: Geremia, S.]]
+
[[Category: Geremia S]]
-
[[Category: Petersen, T E.]]
+
[[Category: Petersen TE]]
-
[[Category: Randaccio, L.]]
+
[[Category: Randaccio L]]
-
[[Category: Wuerges, J.]]
+
[[Category: Wuerges J]]
-
[[Category: alpha_6 - alpha_6 barrel]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:03:46 2008''
+

Current revision

Structure of Cobalamin-complexed Bovine Transcobalamin in Monoclinic Crystal Form

PDB ID 2bb6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools