2nml

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of HEF2/ERH at 1.55 A resolution

Structural highlights

2nml is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2i4f. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.55Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ERH_HUMAN May have a role in the cell cycle.

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

Functional complementation screens can identify known or novel proteins with important intracellular activities. We have isolated human enhancer of filamentation 2 (HEF2) in a screen to find human genes that promote pseudohyphal growth in budding yeast. HEF2 is identical to enhancer of rudimentary homolog (ERH), a highly conserved protein of 104 amino acids. In silico protein-interaction mapping implies that HEF2/ERH interacts with transcription factors, cell-cycle regulators, and other proteins shown to enhance filamentous growth in S. cerevisiae, suggesting a context for studies of HEF2/ERH function. To provide a mechanistic basis to study of HEF2/ERH, we have determined the crystal structure of HEF2/ERH at 1.55 A. The crystal asymmetric unit contains a HEF2/ERH monomer. The two monomers of the physiological dimer are related by the y, x, -z crystal symmetric operation. The HEF2/ERH structure is characterized by a novel alpha + beta fold, a four-strand antiparallel beta-sheet with three alpha-helixes on one side of the sheet. The beta-sheets from the two monomers together constitute a pseudo-beta-barrel, and form the center of the functional HEF2/ERH dimer, with a cavity channel at the dimer interface. Docking of this structure to the HEF2/ERH partner protein DCOH/PCD suggests that HEF2/ERH may regulate the oligomeric state of this protein. These data suggest that HEF2/ERH may be an important transcription regulator that also functions in the control of cell-cycle progression.

A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks.,Jin T, Guo F, Serebriiskii IG, Howard A, Zhang YZ Proteins. 2007 Aug 1;68(2):427-37. PMID:17444515^[1]

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

References

↑ Jin T, Guo F, Serebriiskii IG, Howard A, Zhang YZ. A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks. Proteins. 2007 Aug 1;68(2):427-37. PMID:17444515 doi:http://dx.doi.org/10.1002/prot.21343

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/2nml"

@@ Line 1: / Line 1: @@
 ==Crystal structure of HEF2/ERH at 1.55 A resolution==
-<StructureSection load='2nml' size='340' side='right' caption='[[2nml]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='2nml' size='340' side='right'caption='[[2nml]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2nml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2i4f 2i4f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NML FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2nml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2i4f 2i4f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NML FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</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=2nml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nml OCA], [http://pdbe.org/2nml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nml RCSB], [http://www.ebi.ac.uk/pdbsum/2nml PDBsum]</span></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=2nml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nml OCA], [https://pdbe.org/2nml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nml RCSB], [https://www.ebi.ac.uk/pdbsum/2nml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nml ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ERH_HUMAN ERH_HUMAN]] May have a role in the cell cycle.
+[https://www.uniprot.org/uniprot/ERH_HUMAN ERH_HUMAN] May have a role in the cell cycle.
 == 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/nm/2nml_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/2nml_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2nml ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Guo, F]]
+[[Category: Large Structures]]
-[[Category: Howard, A J]]
+[[Category: Guo F]]
-[[Category: Jin, T C]]
+[[Category: Howard AJ]]
-[[Category: Serebriiskii, I G]]
+[[Category: Jin TC]]
-[[Category: Zhang, Y Z]]
+[[Category: Serebriiskii IG]]
-[[Category: Cell cycle]]
+[[Category: Zhang YZ]]
-[[Category: Hef2/erh fold]]
-[[Category: Interaction network]]
-[[Category: Pseudo beta barrel]]
-[[Category: Transcription]]

2nml

From Proteopedia

Current revision

Crystal structure of HEF2/ERH at 1.55 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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