2blm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="2blm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2blm, resolution 2.0Å" /> '''BETA-LACTAMASE OF BAC...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2blm.jpg|left|200px]]<br /><applet load="2blm" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2blm, resolution 2.0&Aring;" />
'''BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION'''<br />


==Overview==
==BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION==
Two crystal forms (A and B) of the 29,500 Da Class A beta-lactamase, (penicillinase) from Bacillus licheniformis 749/C have been examined, crystallographically. The structure of B-form crystals has been solved to, 2 A resolution, the starting model for which was a 3.5 A structure, obtained from A-form crystals. The beta-lactamase has an alpha + beta, structure with 11 helices and 5 beta-strands seen also in a penicillin, target DD-peptidase of Streptomyces R61. Atomic parameters of the two, molecules in the asymmetric unit were refined by simulated annealing at, 2.0 A resolution. The R factor is 0.208 for the 27,330 data greater than 3, sigma (F), with water molecules excluded from the model. The catalytic, Ser-70 is at the N-terminus of a helix and is within hydrogen bonding, distance of conserved Lys-73. Also interacting with the Lys-73 are Asn-132, and the conserved Glu-166, which is on a potentially flexible, helix-containing loop. The structure suggests the binding of beta-lactam, substrates is facilitated by interactions with Lys-234, Thr-235, and, Ala-237 in a conserved beta-strand peptide, which is antiparallel to the, beta-lactam's acylamido linkage; an exposed cavity near Asn-170 exists for, acylamido substituents. The reactive double bond of clavulanate-type, inhibitors may interact with Arg-244 on the fourth beta-strand. A very, similar binding site architecture is seen in the DD-peptidase.
<StructureSection load='2blm' size='340' side='right'caption='[[2blm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2blm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BLM 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&#8491;</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=2blm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2blm OCA], [https://pdbe.org/2blm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2blm RCSB], [https://www.ebi.ac.uk/pdbsum/2blm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2blm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLAC_BACLI BLAC_BACLI]
== 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/bl/2blm_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=2blm ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2BLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BLM OCA].
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution., Moews PC, Knox JR, Dideberg O, Charlier P, Frere JM, Proteins. 1990;7(2):156-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2326252 2326252]
[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Dideberg O]]
[[Category: Dideberg, O.]]
[[Category: Knox JR]]
[[Category: Knox, J.R.]]
[[Category: Moews PC]]
[[Category: Moews, P.C.]]
[[Category: hydrolase(acting in cyclic amides)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:49:41 2007''

Latest revision as of 09:17, 14 February 2024

BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION

2blm, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2blm&oldid=4058017"