This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1cma

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:43, 7 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1cma.jpg|left|200px]]
 
-
{{Structure
+
==MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE==
-
|PDB= 1cma |SIZE=350|CAPTION= <scene name='initialview01'>1cma</scene>, resolution 2.800&Aring;
+
<StructureSection load='1cma' size='340' side='right'caption='[[1cma]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>
+
<table><tr><td colspan='2'>[[1cma]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMA FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cma OCA], [https://pdbe.org/1cma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cma RCSB], [https://www.ebi.ac.uk/pdbsum/1cma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cma ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cma OCA], [http://www.ebi.ac.uk/pdbsum/1cma PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cma RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/METJ_ECOLI METJ_ECOLI] This regulatory protein, when combined with SAM (S-adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated.[HAMAP-Rule:MF_00744]
 +
== 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/cm/1cma_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=1cma ConSurf].
 +
<div style="clear:both"></div>
-
'''MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE'''
+
==See Also==
-
 
+
*[[Met repressor|Met repressor]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein beta-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs.
+
-
 
+
-
==About this Structure==
+
-
1CMA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMA OCA].
+
-
 
+
-
==Reference==
+
-
Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands., Somers WS, Phillips SE, Nature. 1992 Oct 1;359(6394):387-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1406951 1406951]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Phillips, S E.V.]]
+
[[Category: Phillips SEV]]
-
[[Category: Somers, W S.]]
+
[[Category: Somers WS]]
-
[[Category: double helix]]
+
-
[[Category: protein-dna complex]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:33 2008''
+

Current revision

MET REPRESSOR/DNA COMPLEX + S-ADENOSYL-METHIONINE

PDB ID 1cma

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/1cma"
Personal tools