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1lmb

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Revision as of 06:46, 18 August 2021

REFINED 1.8 ANGSTROM CRYSTAL STRUCTURE OF THE LAMBDA REPRESSOR-OPERATOR COMPLEX

Structural highlights

1lmb is a 4 chain structure with sequence from Enterobacteria phage lambda. This structure supersedes the now removed PDB entry 1lrd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RPC1_LAMBD] Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the lambda repressor-operator complex has been refined to an R-factor of 18.9% at 1.8 A resolution. This refinement, using data collected at low temperature, has revealed the structure of the N-terminal arm and shows that the interactions of repressor with the two halves of the pseudo-symmetric operator site are significantly different. The two halves of the complex are most similar near the outer edge of the operator site (in a region where the lambda and 434 repressors make similar contacts), but they become increasingly different toward the center of the operator. There are striking differences near the center of the site where it appears that the arm makes significant contacts to only one half of the DNA site. This suggested a new way of aligning the operator sites in phage lambda. The high resolution structure confirms many of the previously noted features of the complex, but also reveals a number of new protein-DNA contacts. It also gives a better view of the extensive H-bonding networks that couple contacts made by different residues and different regions of the protein, and reveals important new details about the helix-turn-helix (HTH) region, and the positions of many water molecules in the complex.

Refined 1.8 A crystal structure of the lambda repressor-operator complex.,Beamer LJ, Pabo CO J Mol Biol. 1992 Sep 5;227(1):177-96. PMID:1387915^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Beamer LJ, Pabo CO. Refined 1.8 A crystal structure of the lambda repressor-operator complex. J Mol Biol. 1992 Sep 5;227(1):177-96. PMID:1387915

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lmb"

@@ Line 3: / Line 3: @@
 <StructureSection load='1lmb' size='340' side='right'caption='[[1lmb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lmb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lrd 1lrd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LMB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lmb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lrd 1lrd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMB FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmb OCA], [http://pdbe.org/1lmb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lmb RCSB], [http://www.ebi.ac.uk/pdbsum/1lmb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmb ProSAT]</span></td></tr>
+</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=1lmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmb OCA], [https://pdbe.org/1lmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmb RCSB], [https://www.ebi.ac.uk/pdbsum/1lmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RPC1_LAMBD RPC1_LAMBD]] Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development.
+[[https://www.uniprot.org/uniprot/RPC1_LAMBD RPC1_LAMBD]] Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 </div>
 <div class="pdbe-citations 1lmb" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Bacteriophage repressor 3D structures|Bacteriophage repressor 3D structures]]
-*[[Lambda repressor|Lambda repressor]]
 == References ==
 <references/>

1lmb

From Proteopedia

Revision as of 06:46, 18 August 2021

REFINED 1.8 ANGSTROM CRYSTAL STRUCTURE OF THE LAMBDA REPRESSOR-OPERATOR COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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