2zzi: Difference between revisions

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[[Image:2zzi.png|left|200px]]


{{STRUCTURE_2zzi| PDB=2zzi | SCENE= }}
==Crystal structure of TTHA1623 in a di-iron-bound form==
<StructureSection load='2zzi' size='340' side='right'caption='[[2zzi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2zzi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZZI FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=2zzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzi OCA], [https://pdbe.org/2zzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zzi RCSB], [https://www.ebi.ac.uk/pdbsum/2zzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zzi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5SHV7_THET8 Q5SHV7_THET8]
== 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/zz/2zzi_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=2zzi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.


===Crystal structure of TTHA1623 in a di-iron-bound form===
Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.,Yamamura A, Okada A, Kameda Y, Ohtsuka J, Nakagawa N, Ebihara A, Nagata K, Tanokura M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):455-9. Epub 2009 Apr 24. PMID:19407375<ref>PMID:19407375</ref>


{{ABSTRACT_PUBMED_19407375}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2zzi" style="background-color:#fffaf0;"></div>
[[2zzi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZZI OCA].


==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019407375</ref><references group="xtra"/>
__TOC__
[[Category: Thermus thermophilus]]
</StructureSection>
[[Category: Ebihara, A.]]
[[Category: Large Structures]]
[[Category: Kameda, Y.]]
[[Category: Thermus thermophilus HB8]]
[[Category: Kuramitsu, S.]]
[[Category: Ebihara A]]
[[Category: Nagata, K.]]
[[Category: Kameda Y]]
[[Category: Nakagawa, N.]]
[[Category: Kuramitsu S]]
[[Category: Ohtsuka, J.]]
[[Category: Nagata K]]
[[Category: Okada, A.]]
[[Category: Nakagawa N]]
[[Category: Tanokura, M.]]
[[Category: Ohtsuka J]]
[[Category: Yamamura, A.]]
[[Category: Okada A]]
[[Category: Yokoyama, S.]]
[[Category: Tanokura M]]
[[Category: Hydrolase]]
[[Category: Yamamura A]]
[[Category: Metallo-beta-lactamase]]
[[Category: Yokoyama S]]

Latest revision as of 17:04, 1 November 2023

Crystal structure of TTHA1623 in a di-iron-bound formCrystal structure of TTHA1623 in a di-iron-bound form

Structural highlights

2zzi is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5SHV7_THET8

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

TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.

Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.,Yamamura A, Okada A, Kameda Y, Ohtsuka J, Nakagawa N, Ebihara A, Nagata K, Tanokura M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):455-9. Epub 2009 Apr 24. PMID:19407375[1]

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

See Also

References

  1. ↑ Yamamura A, Okada A, Kameda Y, Ohtsuka J, Nakagawa N, Ebihara A, Nagata K, Tanokura M. Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):455-9. Epub 2009 Apr 24. PMID:19407375 doi:10.1107/S174430910901361X

2zzi, resolution 2.80Å

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