2hi2

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution

Structural highlights

2hi2 is a 1 chain structure with sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FMM1_NEIGO This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells.

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

Type IV pili (T4P) are long, thin, flexible filaments on bacteria that undergo assembly-disassembly from inner membrane pilin subunits and exhibit astonishing multifunctionality. Neisseria gonorrhoeae (gonococcal or GC) T4P are prototypic virulence factors and immune targets for increasingly antibiotic-resistant human pathogens, yet detailed structures are unavailable for any T4P. Here, we determined a detailed experimental GC-T4P structure by quantitative fitting of a 2.3 A full-length pilin crystal structure into a 12.5 A resolution native GC-T4P reconstruction solved by cryo-electron microscopy (cryo-EM) and iterative helical real space reconstruction. Spiraling three-helix bundles form the filament core, anchor the globular heads, and provide strength and flexibility. Protruding hypervariable loops and posttranslational modifications in the globular head shield conserved functional residues in pronounced grooves, creating a surprisingly corrugated pilus surface. These results clarify T4P multifunctionality and assembly-disassembly while suggesting unified assembly mechanisms for T4P, archaeal flagella, and type II secretion system filaments.

Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions.,Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA Mol Cell. 2006 Sep 1;23(5):651-62. PMID:16949362^[1]

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

References

↑ Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA. Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions. Mol Cell. 2006 Sep 1;23(5):651-62. PMID:16949362 doi:10.1016/j.molcel.2006.07.004

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hi2"

Categories: Large Structures | Neisseria gonorrhoeae | Arvai AS | Craig L | Tainer JA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2hi2.png|left|200px]]
-<!--
+==Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution==
-The line below this paragraph, containing "STRUCTURE_2hi2", creates the "Structure Box" on the page.
+<StructureSection load='2hi2' size='340' side='right'caption='[[2hi2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2hi2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HI2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DT6:2,4-BIS(ACETYLAMINO)-2,4-DIDEOXY-BETA-D-GLUCOPYRANOSE'>DT6</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene>, <scene name='pdbligand=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</scene></td></tr>
-{{STRUCTURE_2hi2|  PDB=2hi2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hi2 OCA], [https://pdbe.org/2hi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2hi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hi2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FMM1_NEIGO FMM1_NEIGO] This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells.
+== 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/hi/2hi2_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=2hi2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Type IV pili (T4P) are long, thin, flexible filaments on bacteria that undergo assembly-disassembly from inner membrane pilin subunits and exhibit astonishing multifunctionality. Neisseria gonorrhoeae (gonococcal or GC) T4P are prototypic virulence factors and immune targets for increasingly antibiotic-resistant human pathogens, yet detailed structures are unavailable for any T4P. Here, we determined a detailed experimental GC-T4P structure by quantitative fitting of a 2.3 A full-length pilin crystal structure into a 12.5 A resolution native GC-T4P reconstruction solved by cryo-electron microscopy (cryo-EM) and iterative helical real space reconstruction. Spiraling three-helix bundles form the filament core, anchor the globular heads, and provide strength and flexibility. Protruding hypervariable loops and posttranslational modifications in the globular head shield conserved functional residues in pronounced grooves, creating a surprisingly corrugated pilus surface. These results clarify T4P multifunctionality and assembly-disassembly while suggesting unified assembly mechanisms for T4P, archaeal flagella, and type II secretion system filaments.
-===Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution===
+Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions.,Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA Mol Cell. 2006 Sep 1;23(5):651-62. PMID:16949362<ref>PMID:16949362</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2hi2" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16949362}}, adds the Publication Abstract to the page
+*[[Pilin 3D structures|Pilin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16949362 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16949362}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-HI2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HI2 OCA].
-==Reference==
-Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions., Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA, Mol Cell. 2006 Sep 1;23(5):651-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16949362 16949362]
 [[Category: Neisseria gonorrhoeae]]
-[[Category: Single protein]]
+[[Category: Arvai AS]]
-[[Category: Arvai, A S.]]
+[[Category: Craig L]]
-[[Category: Craig, L.]]
+[[Category: Tainer JA]]
-[[Category: Tainer, J A.]]
-[[Category: Contractile protein]]
-[[Category: Dna binding protein]]
-[[Category: Fiber-forming protein]]
-[[Category: Membrane protein]]
-[[Category: Type iv pilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:32:48 2008''

2hi2

From Proteopedia

Current revision

Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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