2dxu: Difference between revisions

Revision as of 13:01, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2dxu.png

Template:STRUCTURE 2dxu

Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Complexed with Biotinyl-5'-AMP, Mutation R48ACrystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Complexed with Biotinyl-5'-AMP, Mutation R48A

Template:ABSTRACT PUBMED 18372281

About this StructureAbout this Structure

2DXU is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

ReferenceReference

Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate., Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N, J Biol Chem. 2008 May 23;283(21):14739-50. Epub 2008 Mar 26. PMID:18372281

Page seeded by OCA on Sun Jul 27 13:01:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2dxu.gif|left|200px]]
+{{Seed}}
+[[Image:2dxu.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2dxu|  PDB=2dxu  |  SCENE=  }}
-'''Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Complexed with Biotinyl-5'-AMP, Mutation R48A'''
+===Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Complexed with Biotinyl-5'-AMP, Mutation R48A===
-==Overview==
+<!--
-Biotin protein ligase (BPL) catalyzes the biotinylation of the biotin carboxyl carrier protein (BCCP) only at a special lysine residue. Here we report the first structure of BPL.BCCP complex crystals, which are prepared using two BPL mutants: R48A and R48A/K111A. From a detailed structural characterization, it is likely that the mutants retain functionality as enzymes but have a reduced activity to produce the reaction intermediate biotinyl-5'-AMP. The observed biotin and partly disordered ATP in the mutant structures may act as a non-reactive analog of the substrates or biotinyl-5'-AMP, thereby providing the complex crystals. The four crystallographically independent BPL.BCCP complexes obtained can be classified structurally into three groups: the formation stages 1 and 2 with apo-BCCP and the product stage with biotinylated holo-BCCP. Residues responsible for the complex formation as well as for the biotinylation reaction have been identified. The C-terminal domain of BPL shows especially large conformational changes to accommodate BCCP, suggesting its functional importance. The formation stage 1 complex shows the closest distance between the carboxyl carbon of biotin and the special lysine of BCCP, suggesting its relevance to the unobserved reaction stage. Interestingly, bound ATP and biotin are also seen in the product stage, indicating that the substrates may be recruited into the product stage complex before the release of holo-BCCP, probably for the next reaction cycle. The existence of formation and product stages before and after the reaction stage would be favorable to ensure both the reaction efficiency and the extreme substrate specificity of the biotinylation reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_18372281}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18372281 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18372281}}
 ==About this Structure==
@@ Line 36: / Line 40: @@
 [[Category: Structural genomic]]
 [[Category: X-ray diffraction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:28:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:01:36 2008''