2qmo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:28, 17 October 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2qmo.jpg|left|200px]]
 
-
{{Structure
+
==Crystal structure of dethiobiotin synthetase (bioD) from Helicobacter pylori==
-
|PDB= 2qmo |SIZE=350|CAPTION= <scene name='initialview01'>2qmo</scene>, resolution 1.47&Aring;
+
<StructureSection load='2qmo' size='340' side='right'caption='[[2qmo]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
+
<table><tr><td colspan='2'>[[2qmo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QMO FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dethiobiotin_synthase Dethiobiotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.3 6.3.3.3] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47&#8491;</td></tr>
-
|GENE= bioD, HP_0029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Helicobacter pylori 26695])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0132 BioD], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd03109 DTBS]</span>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmo OCA], [https://pdbe.org/2qmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qmo RCSB], [https://www.ebi.ac.uk/pdbsum/2qmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qmo ProSAT], [https://www.topsan.org/Proteins/MCSG/2qmo TOPSAN]</span></td></tr>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmo OCA], [http://www.ebi.ac.uk/pdbsum/2qmo PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2qmo RCSB]</span>
+
</table>
-
}}
+
== Function ==
 +
[https://www.uniprot.org/uniprot/BIOD_HELPY BIOD_HELPY] Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring (By similarity).[HAMAP-Rule:MF_00336]
 +
== 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/qm/2qmo_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2qmo ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Dethiobiotin synthetase (DTBS) is involved in the biosynthesis of biotin in bacteria, fungi, and plants. As humans lack this pathway, DTBS is a promising antimicrobial drug target. We determined structures of DTBS from Helicobacter pylori (hpDTBS) bound with cofactors and a substrate analog, and described its unique characteristics relative to other DTBS proteins. Comparison with bacterial DTBS orthologs revealed considerable structural differences in nucleotide recognition. The C-terminal region of DTBS proteins, which contains two nucleotide-recognition motifs, differs greatly among DTBS proteins from different species. The structure of hpDTBS revealed that this protein is unique and does not contain a C-terminal region containing one of the motifs. The single nucleotide-binding motif in hpDTBS is similar to its counterpart in GTPases; however, isothermal titration calorimetry binding studies showed that hpDTBS has a strong preference for ATP. The structural determinants of ATP specificity were assessed with X-ray crystallographic studies of hpDTBS.ATP and hpDTBS.GTP complexes. The unique mode of nucleotide recognition in hpDTBS makes this protein a good target for H. pylori-specific inhibitors of the biotin synthesis pathway. Database Coordinates and structure factors for structures presented in this article have been deposited in the Protein Data Bank under the following accession codes: 2QMO - apo-form; 3MLE - hpDTBS.8-ac.ADP. in P2(1) 2(1) 2(1) form; 3QXC - hpDTBS.ATP; 3QXH - hpDTBS.8-ac:ADP. in C2 form; 3QXJ - hpDTBS.GTP; 3QXS - hpDTBS.ANP; 3QXX - 8-ac.GDP.; and 3QY0 - hpDTBS.GDP.. Structured digital abstract * hpDTBS and hpDTBS bind by x-ray crystallography (View interaction).
-
'''Crystal structure of dethiobiotin synthetase (bioD) from Helicobacter pylori'''
+
Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members.,Porebski PJ, Klimecka M, Chruszcz M, Nicholls RA, Murzyn K, Cuff ME, Xu X, Cymborowski M, Murshudov GN, Savchenko A, Edwards A, Minor W FEBS J. 2012 Jan 27. doi: 10.1111/j.1742-4658.2012.08506.x. PMID:22284390<ref>PMID:22284390</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2qmo" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
We tested the general applicability of in situ proteolysis to form protein crystals suitable for structure determination by adding a protease (chymotrypsin or trypsin) digestion step to crystallization trials of 55 bacterial and 14 human proteins that had proven recalcitrant to our best efforts at crystallization or structure determination. This is a work in progress; so far we determined structures of 9 bacterial proteins and the human aminoimidazole ribonucleotide synthetase (AIRS) domain.
+
*[[Dethiobiotin synthetase 3D structures|Dethiobiotin synthetase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2QMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QMO OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
In situ proteolysis for protein crystallization and structure determination., Dong A, Xu X, Edwards AM, Chang C, Chruszcz M, Cuff M, Cymborowski M, Di Leo R, Egorova O, Evdokimova E, Filippova E, Gu J, Guthrie J, Ignatchenko A, Joachimiak A, Klostermann N, Kim Y, Korniyenko Y, Minor W, Que Q, Savchenko A, Skarina T, Tan K, Yakunin A, Yee A, Yim V, Zhang R, Zheng H, Akutsu M, Arrowsmith C, Avvakumov GV, Bochkarev A, Dahlgren LG, Dhe-Paganon S, Dimov S, Dombrovski L, Finerty P Jr, Flodin S, Flores A, Graslund S, Hammerstrom M, Herman MD, Hong BS, Hui R, Johansson I, Liu Y, Nilsson M, Nedyalkova L, Nordlund P, Nyman T, Min J, Ouyang H, Park HW, Qi C, Rabeh W, Shen L, Shen Y, Sukumard D, Tempel W, Tong Y, Tresagues L, Vedadi M, Walker JR, Weigelt J, Welin M, Wu H, Xiao T, Zeng H, Zhu H, Nat Methods. 2007 Dec;4(12):1019-21. Epub 2007 Nov 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17982461 17982461]
+
-
[[Category: Dethiobiotin synthase]]
+
[[Category: Helicobacter pylori 26695]]
[[Category: Helicobacter pylori 26695]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Chruszcz, M.]]
+
[[Category: Chruszcz M]]
-
[[Category: Cuff, M.]]
+
[[Category: Cuff M]]
-
[[Category: Cymborowski, M.]]
+
[[Category: Cymborowski M]]
-
[[Category: Edwards, A.]]
+
[[Category: Edwards A]]
-
[[Category: Joachimiak, A.]]
+
[[Category: Joachimiak A]]
-
[[Category: MCSG, Midwest Center for Structural Genomics.]]
+
[[Category: Minor W]]
-
[[Category: Minor, W.]]
+
[[Category: Savchenko A]]
-
[[Category: Savchenko, A.]]
+
[[Category: Xu X]]
-
[[Category: Xu, X.]]
+
[[Category: Zheng H]]
-
[[Category: Zheng, H.]]
+
-
[[Category: atp-binding]]
+
-
[[Category: biotin biosynthesis]]
+
-
[[Category: dethiobiotin synthetase]]
+
-
[[Category: ligase]]
+
-
[[Category: magnesium]]
+
-
[[Category: mcsg]]
+
-
[[Category: midwest center for structural genomic]]
+
-
[[Category: nucleotide-binding]]
+
-
[[Category: protein structure initiative]]
+
-
[[Category: psi-2]]
+
-
[[Category: structural genomic]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:43:25 2008''
+

Current revision

Crystal structure of dethiobiotin synthetase (bioD) from Helicobacter pylori

PDB ID 2qmo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools