PDBsum entry 1s4c

Structural genomics, unknown function

PDB id

1s4c

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Contents

			Protein chains

					150 a.a. *


					147 a.a. *


					140 a.a. *

			Ligands

					ACT

			Metals

					_CU ×4

			Waters ×154

* Residue conservation analysis

PDB id:

1s4c

Links

Name:

Structural genomics, unknown function

Title:

Yhch protein (hi0227) copper complex

Structure:

Protein hi0227. Chain: a, b, c, d. Engineered: yes

Source:

Haemophilus influenzae. Organism_taxid: 727. Gene: hi0227. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.20Å

R-factor:

0.180

R-free:

0.246

Authors:

A.Teplyakov,G.Obmolova,J.Toedt,G.L.Gilliland

Key ref:

A.Teplyakov et al. (2005). Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism. J Bacteriol, 187, 5520-5527. PubMed id: 16077096

Date:

15-Jan-04

Release date:

14-Jun-05

PROCHECK

	Headers

	References

Protein chains

P44583 (Y227_HAEIN) - N-acetylneuraminate anomerase from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Seq: Struc:					155 a.a. 150 a.a.

Protein chain

P44583 (Y227_HAEIN) - N-acetylneuraminate anomerase from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Seq: Struc:					155 a.a. 147 a.a.

Protein chain

P44583 (Y227_HAEIN) - N-acetylneuraminate anomerase from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Seq: Struc:					155 a.a. 140 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	J Bacteriol 187:5520-5527 (2005)
PubMed id: 16077096

Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism.
A.Teplyakov, G.Obmolova, J.Toedt, M.Y.Galperin, G.L.Gilliland.

ABSTRACT

The yhcH gene is part of the nan operon in bacteria that encodes proteins involved in sialic acid catabolism. Determination of the crystal structure of YhcH from Haemophilus influenzae was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. The structure was determined at 2.2-A resolution by multiple-wavelength anomalous diffraction. The protein fold is a variation of the double-stranded beta-helix. Two antiparallel beta-sheets form a funnel opened at one side, where a putative active site contains a copper ion coordinated to the side chains of two histidine and two carboxylic acid residues. A comparison to other proteins with a similar fold and analysis of the genomic context suggested that YhcH may be a sugar isomerase involved in processing of exogenous sialic acid.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20100283

E.Severi, A.H.Hosie, J.A.Hawkhead, and G.H.Thomas (2010).
Characterization of a novel sialic acid transporter of the sodium solute symporter (SSS) family and in vivo comparison with known bacterial sialic acid transporters.

FEMS Microbiol Lett, 304, 47-54.

20349183

M.A.Ferrero, and L.R.Aparicio (2010).
Biosynthesis and production of polysialic acids in bacteria.

Appl Microbiol Biotechnol, 86, 1621-1635.

20190043

S.Roy, C.W.Douglas, and G.P.Stafford (2010).
A novel sialic acid utilization and uptake system in the periodontal pathogen Tannerella forsythia.

J Bacteriol, 192, 2285-2293.

19749043

S.M.Steenbergen, J.L.Jirik, and E.R.Vimr (2009).
YjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-acetylneuraminic acid.

J Bacteriol, 191, 7134-7139.

19060153

Y.Kim, X.Wang, Q.Ma, X.S.Zhang, and T.K.Wood (2009).
Toxin-antitoxin systems in Escherichia coli influence biofilm formation through YjgK (TabA) and fimbriae.

J Bacteriol, 191, 1258-1267.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.