2pbg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2pbg.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2pbg", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2pbg|  PDB=2pbg  |  SCENE=  }}
'''6-PHOSPHO-BETA-D-GALACTOSIDASE FORM-B'''


==6-PHOSPHO-BETA-D-GALACTOSIDASE FORM-B==
<StructureSection load='2pbg' size='340' side='right'caption='[[2pbg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pbg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PBG FirstGlance]. <br>
</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=SO4:SULFATE+ION'>SO4</scene></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=2pbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbg OCA], [https://pdbe.org/2pbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pbg RCSB], [https://www.ebi.ac.uk/pdbsum/2pbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LACG_LACLL LACG_LACLL]
== 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/pb/2pbg_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=2pbg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The initial structural model of 6-phospho-beta-galactosidase from Lactococcus lactis was refined to an R-factor of 16.4% (R[free] = 23.6%) to 2.3 A resolution (1 A = 0.1 nm), and the structures of three other crystal forms were solved by molecular replacement. The four structural models are essentially identical. The catalytic center of the enzyme is approximately at the mass center of the molecule and can only be reached through a 20 A long channel, which is observed with an "open" or "closed" entrance. The closed entrance is probably too small for the educt lactose-6-phosphate to enter, but large enough for the first product glucose to leave. Among the presented structures is a complex between an almost inactive mutant and the second product galactose-6-phosphate, which is exclusively bound at side-chains. A superposition (onto the native enzyme) of galactose-6-phosphate as bound to the mutant suggests the geometry of a postulated covalent intermediate. The binding mode of the educt was modeled, starting from the bound galactose-6-phosphate. A tightly fixed tryptophan is used as a chopping-board for splitting the disaccharide, and several other aromatic residues in the active center cavity are likely to participate in substrate transport/binding.


==Overview==
Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis.,Wiesmann C, Hengstenberg W, Schulz GE J Mol Biol. 1997 Jun 27;269(5):851-60. PMID:9223646<ref>PMID:9223646</ref>
The initial structural model of 6-phospho-beta-galactosidase from Lactococcus lactis was refined to an R-factor of 16.4% (R[free] = 23.6%) to 2.3 A resolution (1 A = 0.1 nm), and the structures of three other crystal forms were solved by molecular replacement. The four structural models are essentially identical. The catalytic center of the enzyme is approximately at the mass center of the molecule and can only be reached through a 20 A long channel, which is observed with an "open" or "closed" entrance. The closed entrance is probably too small for the educt lactose-6-phosphate to enter, but large enough for the first product glucose to leave. Among the presented structures is a complex between an almost inactive mutant and the second product galactose-6-phosphate, which is exclusively bound at side-chains. A superposition (onto the native enzyme) of galactose-6-phosphate as bound to the mutant suggests the geometry of a postulated covalent intermediate. The binding mode of the educt was modeled, starting from the bound galactose-6-phosphate. A tightly fixed tryptophan is used as a chopping-board for splitting the disaccharide, and several other aromatic residues in the active center cavity are likely to participate in substrate transport/binding.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2PBG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBG OCA].
</div>
<div class="pdbe-citations 2pbg" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis., Wiesmann C, Hengstenberg W, Schulz GE, J Mol Biol. 1997 Jun 27;269(5):851-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9223646 9223646]
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
[[Category: 6-phospho-beta-galactosidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Schulz, G E.]]
[[Category: Schulz GE]]
[[Category: Wiesmann, C.]]
[[Category: Wiesmann C]]
[[Category: Glycosyl hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:46:41 2008''