This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3bg9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:28, 21 February 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3bg9.jpg|left|200px]]
 
-
<!--
+
==Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant==
-
The line below this paragraph, containing "STRUCTURE_3bg9", creates the "Structure Box" on the page.
+
<StructureSection load='3bg9' size='340' side='right'caption='[[3bg9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3bg9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BG9 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-
{{STRUCTURE_3bg9| PDB=3bg9 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bg9 OCA], [https://pdbe.org/3bg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bg9 RCSB], [https://www.ebi.ac.uk/pdbsum/3bg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bg9 ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/PYC_HUMAN PYC_HUMAN] Defects in PC are the cause of pyruvate carboxylase deficiency (PC deficiency) [MIM:[https://omim.org/entry/266150 266150]. PC deficiency leads to lactic acidosis, mental retardation and death. It occurs in three forms: mild or type A, severe neonatal or type B, and a very mild lacticacidemia.
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PYC_HUMAN PYC_HUMAN] Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/3bg9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3bg9 ConSurf].
 +
<div style="clear:both"></div>
-
'''Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant'''
+
==See Also==
-
 
+
*[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
Pyruvate carboxylase (PC) catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes. PC contains the biotin carboxylase (BC), carboxyltransferase (CT) and biotin-carboxyl carrier protein (BCCP) domains. We report here the crystal structures at 2.8-A resolution of full-length PC from Staphylococcus aureus and the C-terminal region (missing only the BC domain) of human PC. A conserved tetrameric association is observed for both enzymes, and our structural and mutagenesis studies reveal a previously uncharacterized domain, the PC tetramerization (PT) domain, which is important for oligomerization. A BCCP domain is located in the active site of the CT domain, providing the first molecular insights into how biotin participates in the carboxyltransfer reaction. There are dramatic differences in domain positions in the monomer and the organization of the tetramer between these enzymes and the PC from Rhizobium etli.
+
-
 
+
-
==Disease==
+
-
Known disease associated with this structure: Pyruvate carboxylase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608786 608786]]
+
-
 
+
-
==About this Structure==
+
-
3BG9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BG9 OCA].
+
-
 
+
-
==Reference==
+
-
Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction., Xiang S, Tong L, Nat Struct Mol Biol. 2008 Mar;15(3):295-302. Epub 2008 Feb 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18297087 18297087]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Pyruvate carboxylase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Tong L]]
-
[[Category: Tong, L.]]
+
[[Category: Xiang S]]
-
[[Category: Xiang, S.]]
+
-
[[Category: Atp-binding]]
+
-
[[Category: Biotin]]
+
-
[[Category: Disease mutation]]
+
-
[[Category: Gluconeogenesis]]
+
-
[[Category: Ligase]]
+
-
[[Category: Lipid synthesis]]
+
-
[[Category: Manganese]]
+
-
[[Category: Mitochondrion]]
+
-
[[Category: Multifunctional enzyme]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Tim barrel]]
+
-
[[Category: Transit peptide]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:38:26 2008''
+

Current revision

Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant

PDB ID 3bg9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bg9"
Personal tools