1hcr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:27, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hcr.jpg|left|200px]]
 
-
{{Structure
+
==HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR AND MINOR GROOVE INTERACTIONS==
-
|PDB= 1hcr |SIZE=350|CAPTION= <scene name='initialview01'>1hcr</scene>, resolution 2.300&Aring;
+
<StructureSection load='1hcr' size='340' side='right'caption='[[1hcr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1hcr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCR 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]] 2.3&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcr OCA], [https://pdbe.org/1hcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hcr RCSB], [https://www.ebi.ac.uk/pdbsum/1hcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hcr ProSAT]</span></td></tr>
-
}}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HIN_SALTY HIN_SALTY] A DNA fragment of approximately 900 base pairs, adjacent to the fljB (H2) gene, which specifies the synthesis of phase-2 flagellin, can exist in either orientation with respect to fljB. The orientation of the inversion region controls expression of fljB. The hin gene occupies about two-thirds of the inversion region; it is required for the inversion of the fljB controlling region.
 +
== 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/hc/1hcr_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=1hcr ConSurf].
 +
<div style="clear:both"></div>
-
'''HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR AND MINOR GROOVE INTERACTIONS'''
+
==See Also==
-
 
+
*[[Resolvase 3D structures|Resolvase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
The structure of the 52-amino acid DNA-binding domain of the prokaryotic Hin recombinase, complexed with a DNA recombination half-site, has been solved by x-ray crystallography at 2.3 angstrom resolution. The Hin domain consists of a three-alpha-helix bundle, with the carboxyl-terminal helix inserted into the major groove of DNA, and two flanking extended polypeptide chains that contact bases in the minor groove. The overall structure displays features resembling both a prototypical bacterial helix-turn-helix and the eukaryotic homeodomain, and in many respects is an intermediate between these two DNA-binding motifs. In addition, a new structural motif is seen: the six-amino acid carboxyl-terminal peptide of the Hin domain runs along the minor groove at the edge of the recombination site, with the peptide backbone facing the floor of the groove and side chains extending away toward the exterior. The x-ray structure provides an almost complete explanation for DNA mutant binding studies in the Hin system and for DNA specificity observed in the Hin-related family of DNA invertases.
+
[[Category: Large Structures]]
-
 
+
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
-
==About this Structure==
+
[[Category: Dickerson RE]]
-
1HCR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCR OCA].
+
[[Category: Feng J-A]]
-
 
+
[[Category: Johnson RC]]
-
==Reference==
+
-
Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions., Feng JA, Johnson RC, Dickerson RE, Science. 1994 Jan 21;263(5145):348-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8278807 8278807]
+
-
[[Category: Single protein]]
+
-
[[Category: Dickerson, R E.]]
+
-
[[Category: Feng, J A.]]
+
-
[[Category: Johnson, R C.]]
+
-
[[Category: protein-dna complex]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:22 2008''
+

Current revision

HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR AND MINOR GROOVE INTERACTIONS

PDB ID 1hcr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools