1buc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:39, 7 February 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1buc.gif|left|200px]]
 
-
<!--
+
==THREE-DIMENSIONAL STRUCTURE OF BUTYRYL-COA DEHYDROGENASE FROM MEGASPHAERA ELSDENII==
-
The line below this paragraph, containing "STRUCTURE_1buc", creates the "Structure Box" on the page.
+
<StructureSection load='1buc' size='340' side='right'caption='[[1buc]], [[Resolution|resolution]] 2.50&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'>[[1buc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Megasphaera_elsdenii Megasphaera elsdenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BUC 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]] 2.5&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-
{{STRUCTURE_1buc| PDB=1buc | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1buc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1buc OCA], [https://pdbe.org/1buc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1buc RCSB], [https://www.ebi.ac.uk/pdbsum/1buc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1buc ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ACDS_MEGEL ACDS_MEGEL] Has an optimum specificity for 4-carbon length fatty acyl-CoAs.
 +
== 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/bu/1buc_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=1buc ConSurf].
 +
<div style="clear:both"></div>
-
'''THREE-DIMENSIONAL STRUCTURE OF BUTYRYL-COA DEHYDROGENASE FROM MEGASPHAERA ELSDENII'''
+
==See Also==
-
 
+
*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
The crystal structure of butyryl-CoA dehydrogenase (BCAD) from Megasphaera elsdenii complexed with acetoacetyl-CoA has been solved at 2.5 A resolution. The enzyme crystallizes in the P422 space group with cell dimensions a = b = 107.76 A and c = 153.67 A. BCAD is a bacterial analog of short chain acyl-CoA dehydrogenase from mammalian mitochondria. Mammalian acyl-CoA dehydrogenases are flavin adenine dinucleotide (FAD)-containing enzymes that catalyze the first step in the beta-oxidation of fatty acids. Although specific for substrate chain lengths, they exhibit high sequence homology. The structure of BCAD was solved by the molecular replacement method using the atomic coordinates of pig liver medium chain acyl-CoA dehydrogenase (MCAD). The structure was refined to an R-factor of 19.3%. The overall polypeptide fold of BCAD is similar to that of MCAD. E367 in BCAD is at the same position and in a similar conformation as the catalytic base in MCAD, E376. The main enzymatic differences between BCAD and MCAD are their substrate specificities and the significant oxygen reactivity exhibited by BCAD but not by MCAD. The substrate binding cavity of BCAD is relatively shallow compared to that of MCAD, as consequences of both a single amino acid insertion and differences in the side chains of the helices that make the binding site. The si-face of the FAD in BCAD is more exposed to solvent than that in MCAD. Therefore solvation can stabilize the superoxide anion and considerably increase the rate of oxidation of reduced flavin in the bacterial enzyme.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
1BUC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Megasphaera_elsdenii Megasphaera elsdenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUC OCA].
+
-
 
+
-
==Reference==
+
-
Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii., Djordjevic S, Pace CP, Stankovich MT, Kim JJ, Biochemistry. 1995 Feb 21;34(7):2163-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7857927 7857927]
+
-
[[Category: Butyryl-CoA dehydrogenase]]
+
[[Category: Megasphaera elsdenii]]
[[Category: Megasphaera elsdenii]]
-
[[Category: Single protein]]
+
[[Category: Djordjevic S]]
-
[[Category: Djordjevic, S.]]
+
[[Category: Kim JJP]]
-
[[Category: Kim, J J.P.]]
+
[[Category: Pace CP]]
-
[[Category: Pace, C P.]]
+
[[Category: Stankovich MT]]
-
[[Category: Stankovich, M T.]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:57:55 2008''
+

Current revision

THREE-DIMENSIONAL STRUCTURE OF BUTYRYL-COA DEHYDROGENASE FROM MEGASPHAERA ELSDENII

PDB ID 1buc

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/1buc"
Personal tools